Method for designing a compound based on the three dimensional structure of phosphoinositide dependent protein kinase 1 (PDK1)

ABSTRACT

A method for selecting a compound for modulating the activity of phosphoinositide dependent protein kinase 1 (PDKI) is provided. The method may comprise modelling a three dimensional structure of a plurality of molecules in a computer, comparing with the three dimensional structure of the compounds with that of a reference structure such as at least part of a protein kinase catalytic domain of PDK1, and selecting the compound based on a predicted interacting ability of the molecules to the protein kinase catalytic domain. Also a method for selecting a compound for modulating the activity of hydrophobic pocket containing protein kinase is provided. In this method, the reference structures may be one or more of a phosphate binding pocket of PDK1, a hydrophobic pocket of PDK1, and αC helix or region interacting therewith of PDK1.

CROSS-REFERENCE TO RELATED APPLICATION

The present application is the US national phase under 35 USC 371 of International Application No. PCT/GB03/02509, filed Jun. 9, 2003, and published in the English language as WO 03/104481.

REFERENCE TO SEQUENCE LISTING

The present application incorporates by reference the sequence listing submitted as an ASCII text filed via EFS-Web on Feb. 5, 2010. The Sequence Listing is provided as a file entitled 8506534.1.txt, created on-Feb. 5, 2010, which is 4 Kb in size.

FIELD OF THE INVENTION

The present invention relates to protein kinase catalytic domain structures and mutants and screening assays making use thereof.

BACKGROUND OF THE INVENTION

The 3-Phosphoinositide Dependent Protein Kinase-1 (PDK1) is a key protein kinase, regulating activity of a group of related protein kinases through phosphorylation. These kinases include isoforms of Protein Kinase B (also known as Akt) [Brazil and Hemmings, 2001, Scheid and Woodgett, 2001], p70 ribosomal S6 kinase (S6K) [Alessi et al., 1997, Volarevic and Thomas, 2001], p90 ribosomal S6 Kinase (RSK) [Frodin and Gammeltoft, 1999] and the serum and glucocorticoid induced-protein kinase (SGK) [Lang and Cohen, 2001]. These enzymes are stimulated by hormones and growth factors and phosphorylate regulatory proteins mediating the various physiological effects of these agonists.

PDK1 possesses an N-terminal kinase catalytic domain and a C-terminal pleckstrin homology (PH) domain [Alessi et al., 1997, Stephens et al., 1998]. PDK1 activates its substrates by phosphorylating these kinases at their activation loop (reviewed in [Alessi, 2001, Toker and Newton, 2000]). The phosphorylation of PKB by PDK1 is dependent upon prior activation of the phosphoinositide 3-kinase (PI-3-kinase) and the production of the second messenger, phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P₃) which binds to the PH domains of PDK1 and PKB. This does not activate either PKB or PDK1 but instead recruits and co-localises these enzymes at the plasma membrane.

Unlike PKB, the other PDK1 substrates described thus far do not interact with PtdIns(3,4,5)P₃ nor is the rate at which they are phosphorylated by PDK1 further enhanced by the binding of PDK1 to PtdIns(3,4,5)P₃. Instead the ability of PDK1 to phosphorylate S6K, SGK and RSK is promoted by phosphorylation of these enzymes at a residue located C-terminal to the kinase catalytic domain in a region known as the hydrophobic motif [Alessi et al., 1997, Kobayashi and Cohen, 1999, Pullen et al., 1998]. The kinases that phosphorylate the hydrophobic motif of S6K and SGK are unknown but as the phosphorylation of this residue in vivo is dependent on PI-3-kinase activation, the hydrophobic motif kinases and/or the hydrophobic motif phosphatases may be regulated by PtdIns(3,4,5)P₃. In the case of RSK isoforms, phosphorylation by the ERK1/ERK2 MAP kinases induce phosphorylation of the hydrophobic motif (reviewed in Frodin and Gammeltoft, 1999).

PDK1 belongs to the same subfamily of protein kinases as its substrates, termed the AGC protein kinases as they are related to the cAMP dependent protein kinase (PKA)/cGMP dependent protein kinase/Protein kinase C (PKC). PKA is the only AGC kinase whose crystal structure has been solved. Like all protein kinases, its catalytic core possesses an N-terminal lobe consisting mainly of β-sheet and a predominantly α-helical C-terminal lobe [Taylor et al., 1992, Husen and Kuriyan, 2002]. The ATP binding site is located in between the 2 lobes [Johnson et al., 2001, Knighton et al., 1991]. At the very C-terminus, PKA possesses an extended loop that terminates in the sequence FXXF (SEQ ID NO:1) which resembles the first part of the hydrophobic motif phosphorylation site of S6K and SGK (FXXFS/TY, SEQ ID NO:2) in which the Ser/Thr is the phosphorylated residue [Biondi et al., 2000]. In the structure of PKA, the FXXF motif (SEQ ID NO:1) is buried in a hydrophobic pocket in the small lobe of the PKA catalytic domain [Knighton et al., 1991] and mutation of either of the Phe residues drastically reduces PKA activity towards a peptide substrate [Etchebehere et al., 1997]. Unlike other AGC kinases, PDK1 does not possess a hydrophobic motif C-terminal to its catalytic domain. However, there is evidence that PDK1 possesses a hydrophobic pocket in the small lobe of its catalytic domain similar to that in PKA. We have biochemically demonstrated that the interaction of PDK1 with four of its substrates (S6K1, SGK1, PKζ and PKC related kinase-2 (PRK2)) is reduced or abolished by mutation of residues predicted to form part of this pocket [Balendran et al., 2000, Biondi et al., 2000]. Furthermore, mutation of a central residue in the predicted pocket, Leu 155, prevented PDK1 from phosphorylating and activating S6K1 and SGK1 without affecting its ability to phosphorylate either PKB or a short peptide substrate that encompasses the activation loop of PKB (T308tide) [Biondi et al., 2000]. The hydrophobic pocket on the kinase domain of PDK1 has been termed the “PIF-pocket” after the name of the first AGC-kinase hydrophobic motif-containing peptide (PDK1 Interacting Fragment) that was found to bind PDK1 [Balendran et al., 1999a]. It has been suggested that the PIF-pocket in PDK1 functions as a docking site, enabling PDK1 to interact with some of its physiological substrates. Furthermore, there is evidence that phosphorylation of the hydrophobic motif of S6K1, SGK and RSK2 [Balendran et al., 1999b, Biondi et al., 2001, Frodin et al., 2000] promotes the interaction of these enzymes with PDK1. These findings suggest that the PIF-pocket on PDK1 could contain a phosphate binding site promoting the binding of PDK1 to a subset of substrates (S6K, SGK and RSK) once these enzymes have been phosphorylated at their hydrophobic motif. This would result in a physiological phosphate dependent interaction. In addition there is evidence that occupancy of the PIF-pocket activates PDK1 as peptides that encompass the hydrophobic motif of PRK2 [Biondi et al., 2000] and RSK [Frodin et al., 2000] induce a 4-6-fold activation of PDK1.

Previous predicted structures PDK1 catalytic domain were obtained using homology modelling methods based upon structural information available from the catalytic domain of PKA (Biondi et al., 2000). These predictions of the PDK1 catalytic domain structure were thus biased towards the catalytic domain from which the structural information was obtained.

SUMMARY OF THE INVENTION

We have determined a crystal structure for the kinase domain of the AGC family protein kinase PDK. The structure defines the PIF-pocket and reveals an adjacent possible phosphate binding site. Furthermore, we have performed structure-based mutagenesis and biochemical analysis which support the existence of such a phosphate-binding site. This may mediate the phosphate dependent docking interaction with substrates such as (for PDK1) S6K and SGK. We have used a novel algorithm to define the conformational state of the crystallised PDK1 relative to all the reported structures of PKA, which shows that while PDK1 has all the signs of being in an active form in the crystal, its overall conformation is in-between and ‘open’ and ‘closed’ state. We have also determined crystal structures for the kinase domain of PDK1 in complex with modulators of PDK1 activity.

On the basis of this work we provide drug screening methods and mutated protein kinase molecules (which are useful in, for example, drug screening methods).

A first aspect of the invention provides a method for selecting or designing a compound for modulating the activity of phosphoinositide dependent protein kinase 1 (PDK1), the method comprising the step of using molecular modelling means to select or design a compound that is predicted to interact with the protein kinase catalytic domain of PDK1, wherein a three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 is compared with a three-dimensional structure of a compound, and a compound that is predicted to interact with the said protein kinase catalytic domain is selected, wherein the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 is a three-dimensional structure (or part thereof) determined for a polypeptide consisting of residues equivalent to residues 51 to 359 of full length human PDK1, or a fragment or fusion thereof.

BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1 provides an overview of the PDK1 structure.

FIGS. 2A and 2B show the PIF-pocket.

FIG. 3 shows a structure-based sequence alignment

FIGS. 4A-C show PDK1 binding & activation studies.

FIGS. 5A and 5B show interactions of regulatory phosphates with the αC helix.

FIGS. 6A and 6B show essential dynamics.

FIG. 7 shows alignment of AGC protein kinase family members.

FIG. 8 shows staurosporine and UCN-01 electron density.

FIG. 9 shows details of the inhibitor binding sites.

DETAILED DESCRIPTION OF THE INVENTION

The term PDK1 as used herein includes a polypeptide (a PDK1 polypeptide) comprising the amino acid sequence identified as PDK1 in Alessi D. R et al (1997) Curr. Biol. 7: 261-269, Alessi D. R et al (1997) Curr. Biol. 7: 776-789, Stokoe D et al (1997) Science 277: 567-570 or Stephens L et al (1998) Science 279: 710-714, or a variant, fragment, fusion or derivative thereof, or a fusion of a said variant or fragment or derivative, for example as described in WO98/41638, incorporated herein by reference. It is preferred that the said PDK1 polypeptide is a protein kinase. It is preferred that the said PDK1 polypeptide is a protein kinase that is capable of phosphorylating a threonine residue that lies in a Thr-Phe-Cys-Gly-Thr-Xaa-Glu-Leu consensus motif (where the underlined Thr corresponds to the threonine that is phosphorylated by PDK1 and Xaa is a variable residue, SEQ ID NO:9), and preferably that is capable of phosphorylating PKB, for example PKBα, at residue Thr308. The rate at which the said PDK1 polypeptide is capable of phosphorylating a threonine residue as described above may be increased in the presence of PtdIns(3,4,5)P₃ or PtdIns(3,4)P₂ but it will be appreciated that this is not essential. The said polypeptide may be capable of phosphorylating the equivalent residues to Thr308 of PKBα on PKC isoforms (LeGood et al (1998) Science 281: 2042-2045; et al (1998) Curr. Biol. 8: 1069-1077; Dutil et al (1998) Curr. Biol. 8:1366-1375), p70 S6 kinase (Alessi et al (1998) Curr. Biol. 8: 69-81; Pullen et al (1998) Science 279, 707-710), SGK (sequence given in Webster et al (1993) Mol. Cell. Biol. 13, 1031-2040; equivalent residues identified in US application no 112217 filed on 14 Dec. 1998; GB 9919676.8, filed on 19 Aug. 1999, and Kobayashi & Cohen (1999)) and PKA (Cheng et al (1998) Proc. Natl. Acad. Sci. USA 95: 9849-9854). It may further be preferred that the substrate specificity and/or other characteristics of the said PDK1 polypeptide in vitro may be substantially as reported in Alessi D. R et al (1997) Curr. Biol. 7: 261-269, Alessi D. R et al (1997) Curr. Biol. 7: 776-789, Stokoe D et al (1997) Science 277: 567-570 or Stephens L et al (1998) Science 279: 710-714.

We have found that a fragment of PDK1 consisting essentially of residues equivalent to residues 51 to 359 of full length human PDK1 is particularly beneficial for determining a structure for the catalytic domain of PDK1. This fragment has, for example, protein kinase activity and surprisingly beneficial solubility and stability characteristics which make it particularly suitable for structural studies, for example formation of crystals which may be analysed by X-ray crystallography methods. Other fragments of PDK1 were surprisingly found to be unsuitable for crystallisation, as discussed in Example 5.

It is particularly preferred that the structure is one determined for the fragment consisting of residues 51 to 359 of full length human PDK1. The fragment may comprise an N-terminal or C-terminal fusion polypeptide (ie amino acid sequence not derived from PDK1), though this is preferably of less than or equal to about 10, 5, 4, 3, 2 or 1 amino acids. For example, it is particularly preferred that the structure is one determined for a polypeptide consisting residues 51 to 359 of full length human PDK1 and the amino acid sequence Gly-Pro (or less preferably other sequence forming part of a protease cleavage site) preceding the methionine corresponding to Met51 of human PDK1. A further preferred structure is one determined for the fragment consisting essentially of residues 71 to 359 of full length human PDK1 (or residues equivalent thereto), which also has protein kinase activity.

It is particularly preferred that the structure is one determinable by a method as described in Example 1, for example a structure obtainable by X-ray analysis from a crystal obtainable using a mother liquor solution comprising ammonium sulphate, preferably between 1.8 and 2.2M. It is particularly preferred that the mother liquor solution is of pH 7 to 9, preferably 7 to 8.5, most preferably pH8.5, and comprises ammonium sulphate and preferably ATP. Crystals may form in the absence of ATP but better crystals may be obtained in the presence of ATP. Preferably the crystal is obtainable using a mother liquor solution containing 0.1M Tris/HCl pH 8.5, 2.0 M ammonium sulphate, 16.6 mM ATP. Further preferred details of the crystallisation and X-ray analysis are described in Example 1, for example as partially summarised in Table 1 (shown in Example 1).

It is particularly preferred that the structure is that represented by the structure co-ordinates shown in Examples 2, 3 or 4, or a structure based or modelled on such a structure or co-ordinates. The co-ordinates shown in Example 2 are for the PDK1 fragment (SEQ ID NO:102) with all alternate side chains. The co-ordinates shown in Example 3 are for the PDK1 fragment (SEQ ID NO:102) without alternate side chains. The co-ordinates shown in Example 4 are for the dimer of the PDK1 fragment (SEQ ID NO:102), without alternate side chains; chain A is the molecule for which co-ordinates are given in Examples 2 and 3, and chain B is the symmetry-related molecule.

The structure may be one determined following crystallisation in the presence of a known or potential interactor with PDK1 or modulator of PDK1 activity (as discussed further below), for example a known or potential inhibitor of PDK1 activity. For example, the structure may be one determined following crystallisation in the presence of a known protein kinase inhibitor, for example an inhibitor that binds at the ATP binding site, for example an ATP-competitive inhibitor, for example staurosporine or a staurosporine derivative, for example UCN-01. Examples of such crystallisation techniques and analysis are given in Example 6, and examples of co-ordinates are given in Examples 7 and 8. Example 7 represents the co-ordinates of PDK1 fragment (SEQ ID NO:102) co-crystallised with Staurosporine, whereas in Example 8, the co-ordinates of PDK1 fragment (SEQ ID NO:102) co-crystallised with UCN-01.

It will be appreciated that some variation in crystallisation conditions (for example different mother liquors) may be required for co-crystallisation with different molecules. Techniques for investigating suitable crystallisation conditions in each case will be well known to those skilled in the art.

A further aspect of the invention provides a crystalline form of a polypeptide as defined in any of the preceding aspects of the invention, for example a polypeptide consisting of residues equivalent to residues 51 to 359 of full length human PDK1, or a fragment or fusion thereof; a polypeptide consisting of residues 51 to 359 of full length human PDK1 or a fusion thereof; a polypeptide consisting of residues 51 to 359 of full length human PDK1 and the amino acid sequence Gly-Pro preceding the methionine corresponding to Met51 of human PDK1; a polypeptide consisting of residues 71 to 359 of full length human PDK1 or a fusion thereof.

The crystalline form may further comprise co-crystallised molecule, for example a known or potential interactor with PDK1 or modulator of PDK1 activity, or a test compound whose properties vis a vis PDK1 may not be known. For example, the co-crystallised molecule, for example test compound, may be a molecule that is known to modulate protein kinase activity, or may already be known to modulate PDK1 protein kinase activity. For example, the co-crystallised molecule may be staurosporine, the staurosporine derivative UCN-01 (7-hydroxyl staurosporine) or other staurosporine derivative.

Such co-crystallisation and structures determined from co-crystallised molecules may be useful in molecular modelling and in determining features of the polypeptide and compound that are important for interaction. This may be useful in designing or selecting further test compounds, for example as discussed in Example 6.

In one embodiment it is preferred that the modelled molecule is predicted to bind to a region of the structure termed the “PIF binding pocket”, the “phosphate binding pocket” and/or the a C helix (residues equivalent to 123-136 of full length human PDK1), particularly the residue equivalent to Arg 131 of full length human PDK1, or interacting regions. As discussed in Example 1, the PIF binding pocket is considered to be formed by residues including Lys115, Ile118, Ile119 on the αB helix, Val124, Val127 on the αC helix and Leu 155 on 13-sheet 5. The phosphate binding pocket is considered to be formed by residues including Lys76, Arg 131, Thr 148 and Gln150. Residues of the αC helix that are considered to interact either with phosphate bound in the phosphate binding site or intermolecularly with phosphorylated Ser241 of PDK1 include Arg131 (phosphate binding site) and Arg 129 and His126 (phosphorylated Ser241). Glu 130 is involved in binding the α-phosphate of the bound ATP, and Val124 and Val127 form part of the PIF binding pocket, as discussed in Example 1.

It is preferred that the compound is for modulating the protein kinase activity of PDK1. The protein kinase activity of PDK1 that is modulated may be phosphorylation of the underlined residue in a polypeptide with the amino acid sequence Thr/Ser-Phe-Cys-Gly-Thr-Xaa-Glu-Leu (“PDK1” activity, SEQ ID NO:9). Alternatively or in addition, the modulated activity may be phosphorylation of the underlined residue in a polypeptide with the amino acid sequence Phe-Xaa-Xaa-Phe-Ser/Thr-Phe/Tyr (“PDK2” activity, SEQ ID NO:11). The substrate polypeptide may be, for example, a PKB, SGK, p70 S6 kinase, PKC or (in relation only to phosphorylation of the underlined residue in a polypeptide with the amino acid sequence Thr/Ser-Phe-Cys-Gly-Thr-Xaa-Glu-Leu (SEQ ID NO:9) PKA polypeptide. The modulated protein kinase activity may be towards PKB or other PH-domain-comprising/phosphoinositide-binding substrate of PDK1; or SGK, S6K or other substrate of PDK1 whose phosphorylation by PDK1 is promoted by phosphorylation of the substrate on the Ser/Thr of the “hydrophobic motif” FXXFS/TY (SEQ ID NO:2); or an artificial substrate such as T308tide (which comprises the sequence of PKB which is phosphorylated by PDK1) or PDKtide (which comprises the sequence of PKB which is phosphorylated by PDK1 (eg T308tide) fused to a sequence mimicking a phosphorylated hydrophobic motif ie FXXFZY (SEQ ID NO: 2), in which Z is a negatively charged (for example acidic) residue (eg PIFtide)). Such substrates for PDK1 are discussed, for example, in WO 01/44497. Other activities of PDK1 that may be modulated include interactions with other polypeptides or phosphoinositides and/or intramolecular interactions.

It is preferred that the three-dimensional structure of at least a part of the protein kinase catalytic domain of the PDK1 is a three-dimensional structure of at least a part of the PIF binding pocket, the phosphate binding pocket and/or the α C helix, or interacting regions of PDK1, and a compound that is predicted to interact with the said PIF binding pocket, the phosphate binding pocket and/or the α C helix, or interacting regions of PDK1 is selected. Alternatively, the compound may bind to a portion of said PDK1 polypeptide that is not the PIF binding pocket, the phosphate binding pocket and/or the α C helix, or interacting regions of PDK1, for example so as to interfere with the binding of the ATP or substrate polypeptide or their access to the catalytic site. In a still further example, the compound may bind to a portion of PDK1 so as to decrease said polypeptide's activity by an allosteric effect. This allosteric effect may be an allosteric effect that is involved in the natural regulation of PDK1's activity.

It is further preferred that the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 is a three-dimensional structure of the part of the protein kinase catalytic domain of PDK1 that is defined by residues Lys115, Ile118, Ile119 (on the αB helix), Val124, Val127 (on the αC helix) and Leu 155 (on 13-sheet 50 and/or residues Lys76, Arg 131, Thr 148 and Gln150 and/or residues Arg131, Arg 129, His126, Glu 130 of full-length human PDK1 and a compound that is predicted to interact with the said part of the protein kinase catalytic domain is selected.

For example, it is preferred if the portions of the structure of PDK1 shown in FIGS. 1 and 2 as forming the PIF binding pocket and/or phosphate binding pocket and/or αC helix interactions (for example with phosphoserine241) are compared with the structure of the candidate compound.

A further aspect of the invention provides a method for selecting or designing a compound for modulating the activity of a hydrophobic pocket (PIF binding pocket)-containing protein kinase having a hydrophobic pocket in the position equivalent to the hydrophobic pocket of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and/or Leu155 of full-length human PDK1 and further having a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and/or Gln150, the method comprising the step of using molecular modelling means to select or design a compound that is predicted to interact with the said hydrophobic pocket-containing protein kinase, wherein a three-dimensional structure of a compound is compared with a three-dimensional structure of the said phosphate binding pocket and optionally also the hydrophobic pocket and/or αC helix or region interacting therewith, and a compound that is predicted to interact with the said phosphate binding pocket and optionally also the hydrophobic pocket and/or αC helix or region interacting therewith, is selected.

The three-dimensional structure of a compound may be compared with the three-dimensional structure of the hydrophobic and/or phosphate binding pocket and/or αC helix or region interacting therewith, as appropriate. A compound that can interact with the hydrophobic pocket and/or phosphate binding pocket, in particular residues noted above as defining such regions, in a similar manner (for example similar separation and/or type of interaction ie hydrophobic or ionic, and/or similar cumulative energy of interaction) to an interacting polypeptide such as S6K-pHM may be selected. Methods of assessing the interaction are well known to those skilled in the art and are discussed further below.

The three-dimensional structures that are compared may be, as appropriate, predicted or modelled three-dimensional structures (for example on the basis of a PDK1 structure as referred to above, for example as represented by the co-ordinates given in Examples 2, 3 or 4 or 6 or 7) or may be three-dimensional structures that have been determined, for example by techniques such as X-ray crystallography, as well known to those skilled in the art. The three-dimensional structures may be displayed by a computer in a two-dimensional form, for example on a computer screen. The comparison may be performed using such two-dimensional displays.

The following relate to molecular modelling techniques: Blundell et al (1996) Structure-based drug design Nature 384, 23-26; Bohm (1996) Computational tools for structure-based ligand design Prog Biophys Mol Biol 66(3), 197-210; Cohen et al (1990) J Med Chem 33, 883-894; Navia et al (1992) Curr Opin Struct Biol 2, 202-210.

The following computer programs, for example, may be useful in carrying out the method of this aspect of the invention: GRID (Goodford (1985) J Med Chem 28, 849-857; available from Oxford University, Oxford, UK); MCSS (Miranker et al (1991) Proteins: Structure, Function and Genetics 11, 29-34; available from Molecular Simulations, Burlington, Mass.); AUTODOCK (Goodsell et al (1990) Proteins: Structure, Function and Genetics 8, 195-202; available from Scripps Research Institute, La Jolla, Calif.); DOCK (Kuntz et al (1982) J Mol Biol 161, 269-288; available from the University of California, San Francisco, Calif.); LUDI (Bohm (1992) J Comp Aid Molec Design 6, 61-78; available from Biosym Technologies, San Diego, Calif.); LEGEND (Nishibata et al (1991) Tetrahedron 47, 8985; available from Molecular Simulations, Burlington, Mass.); LeapFrog (available from Tripos Associates, St Louis, Mo.); Gaussian 92, for example revision C (M J Frisch, Gaussian, Inc., Pittsburgh, Pa. ©1992); AMBER, version 4.0 (P A Kollman, University of California at San Francisco, ©1994); QUANTA/CHARMM (Molecular Simulations, Inc., Burlington, Mass. ©1994); and Insight II/Discover (Biosym Technologies Inc., San Diego, Calif. ©1994). Programs may be run on, for example, a Silicon Graphics™ workstation, Indigo²™ or IBM RISC/6000™ workstation model 550.

Several in silico methods could be employed, for example, via a substructure search for new ligands using programmes such as CHEM DRAW or CHEM FINDER. The basic structure of the natural ligand (for example a phosphorylated hydrophobic motif peptide such as 56K-pHM) capable of binding to PDK1 (or other protein kinase) is taken (or predicted) and various structural features of it (for example the hydrophobic and negatively charged entities) are submitted to a programme which will searches a set of chemical company catalogues for chemicals containing this substructure.

These compounds are then screened by eye for groups that could not interact with the PIF/phosphate binding pockets (or the αC residues/interacting region) because, for example, they are too large or have steric or charge hindrance, and those are discarded. The remaining chemicals are submitted to a PRODRG server and topologies/co-ordinates for these chemicals are created. These chemicals are modelled into the structure, from which chemicals that are possibly able to bind to the PIF/phosphate binding site domain/αC helix/interacting region are selected. Further details of the PRODRG programme are available in the art, for example, from Daan van Aalten Laboratory.

These compounds may then be ordered or synthesised and assessed, for one or more of ability to bind to and/or modulate PDK1 (or other protein kinase) activity. The compounds may be crystallised with the PDK1 or other protein kinase protein and the structure of any complex determined, as illustrated in Examples 6 to 8.

An alternative approach is to use PRODRG: a tool for generating GROMOS/MOL2/WHATIF topologies and hydrogen atom positions from small molecule PDB files. We take the natural ligand and computationally vary all possible groups at each site on the ligand, with a variety of new groups while the protein co-ordinates and the ligand back-bone co-ordinates remain fixed the results can then be screened for hindrance and repulsion, and the molecules are obtained either through catalogues or made.

As noted above, the selected or designed compound may be synthesised (if not already synthesised) or purified and tested for its effect on the relevant hydrophobic/phosphate pocket-containing protein kinase, for example its effect on the protein kinase activity. The compound may be tested in a screening method of the invention or other screening method. The compound may be formulated for pharmaceutical use, for example for use in in vivo trials in animals or humans, or for use in agriculture, for example as an antifungal agent.

It may be useful to analyse a protein kinase structure (for example a structure determined or predicted for a complex of the protein kinase with a binding partner) in order to determine the activation state of the structure. This may be useful in further modelling binding of the binding partner to the protein kinase in other activation states, and in predicting how the binding partner may affect the activation state of the protein kinase or compete with other potential binding partners. It may also be useful in designing and assessing derivatives of the binding partner.

Thus, a further aspect of the invention provides a method for assessing the activation state of a structure for a protein kinase, wherein the structure is analysed using principle component analysis of the structure co-ordinates. The method may further comprise the step of classifying the activation state of the structure as “open”, “closed” or “intermediate”. Details of the analysis, which involves the generation of eigenvectors and associated eigenvalues are given in Example 1. The analysis makes use of techniques described in Amadei et al (1993) Essential dynamics of proteins. Proteins 17, 412-425.

The hydrophobic/phosphate pocket-containing protein kinase may be PDK1. Alternatively, it may be an isoform of Serum and Glucocorticoid stimulated protein kinase (SGK), Protein Kinase B (PKB), p70 S6 kinase, p90 RSK, PKC isoforms (for example PKCα, PKCδ, PKCζ), PRK1, PRK2, MSK1 or MSK2. Hydrophobic/phosphate pocket-containing protein kinases and their EMBL database accession numbers are listed in Table I. Sequences considered to form the phosphate binding pocket from representative hydrophobic/phosphate pocket-containing protein kinases are shown in FIG. 5. All AGC family protein kinases other than PKA may be hydrophobic/phosphate pocket-containing protein kinases, as defined above. In addition to the protein kinases shown in FIG. 7, rhodopsin and G-protein coupled receptor protein kinases, for example, may possibly also have a hydrophobic/phosphate pocket as defined above.

The terms SGK, PKB, p70 S6 kinase, p90 RSK, PKCα, PKCδ, PKCζ or PRK2, for example, as used herein include a polypeptide (a SGK, PKB, PKA, p70S6 kinase, p90 RSK, PKCα, PKCδ, PKCζ or PRK2 polypeptide) comprising the amino acid sequence identified as a SGK, PKB, p70 S6 kinase, p90 RSK, PKCα, PKCδ, PKCζ or PRK2, respectively, in the relevant EMBL database records indicated in Table 2.

TABLE 2 Activation or AGC Hydrophobic Accession T-Loop Motif number consensus: TFCGTxxYxAPD FxxFSY (SEQ ID NO:41) (SEQ ID NO:42) L E YTF PKBα TFCGTPEYLAPE FPQFSY (Y15056) (SEQ ID NO:45) (SEQ ID NO:46) PKBβ TFCGTPEYLAPE FPQFSY (P31751) (SEQ ID NO:47) (SEQ ID NO:48) PKBγ TFCGTPEYLAPE FPQFSY (AF135794) (SEQ ID NO:49) (SEQ ID NO:50) SGK1 TFCGTPEYLAPE FLGFSY (AAD41091) (SEQ ID NO:51) (SEQ ID NO:52) SGK2 TFCGTPEYLAPE FLGFSY (AF169034) (SEQ ID NO:53) (SEQ ID NO:54) SGK3 TFCGTPEYLAPE FLGFSY (AF169035) (SEQ ID NO:55) (SEQ ID NO:56) PKCα TFCGTPDYIAPE FEGFSY (4506067) (SEQ ID NO:57) (SEQ ID NO:58) PKCβI TFCGTPDYIAPE FAGFSY (4506069) (SEQ ID NO:59) (SEQ ID NO:60) PKCβII TFCGTPDYIAPE FEGFSF (P05127) (SEQ ID NO:61) (SEQ ID NO:62) PKCγ TFCGTPDYIAPE FGGFTY (P05129) (SEQ ID NO:63) (SEQ ID NO:64) PKCδ TFCGTPDYIAPE FAGFSF (5453970) (SEQ ID NO:65) (SEQ ID NO:66) PCKζ TFCGTPNYIAPE FEGFEY (4506079) (SEQ ID NO:67) (SEQ ID NO:68) PKCι TFCGTPNYIAPE FEGFEY (4506071) (SEQ ID NO:69) (SEQ ID NO:68) PRK1 TFCGTPEFLAPE FLDFDF (AAC50209) (SEQ ID NO:71) (SEQ ID NO:72) PRK2 TFCGTPEFLAPE FRDFDY (AAC50208) (SEQ ID NO:73) (SEQ ID NO:74) p70-S6Kα TFCGTIEYMAiPE FLGFTY (AAA36410) (SEQ ID NO:75) (SEQ ID NO:76) p70-S6Kβ TFCGTIEYMAPE FLGFTY (4506739) (SEQ ID NO:77) (SEQ ID NO:78) p90-RSK1 SFCGTVEYMAPE FRGFSF (I38556) (SEQ ID NO:79) (SEQ ID NO:80) p90-RSK2 SFCGTVEYMAPE FRDFSF (P51812) (SEQ ID NO:81) (SEQ ID NO:82) p90-RSK3 SFCGTIEYMAPE FRGFSF (CAA59427) (SEQ ID NO:83) (SEQ ID NO:84) MSK1 SFCGTIEYMAPD FQGYSF (AAC31171) (SEQ ID NO:85) (SEQ ID NO:86) MSK2 SFCGTIEYMAPE FQGYSF (AAC67395) (SEQ ID NO:87) (SEQ ID NO:88) PDK1 SFVGTAQYVSPE (1) (AF017995) (SEQ ID NO:89)

Table 2. Alignment of the amino acid sequences surrounding the T-loop and the hydrophobic motif of AGC kinases. All the sequences and accession numbers are from human proteins. The underlined residues correspond to those that become phosphorylated. Footnotes: (1) PDK1 does not possess a hydrophobic motif.

It is preferred that the PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) is a polypeptide which consists of the amino acid sequence of the protein kinase PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase as the case may be) sequence referred to above or naturally occurring allelic variants thereof. It is preferred that the naturally occurring allelic variants are mammalian, preferably human, but may alternatively be homologues from parasitic or pathogenic or potentially pathogenic organisms. Examples of such organisms and homologues, and of uses of modulators of such homologues are given in U.S. patent application No. 60/112,114, filed on 14 Dec. 1998, and applications claiming priority therefrom, or in Casamayor et al (1999) Curr Biol 9, 186-197.

The PDK1 may also be a polypeptide with the amino acid sequence of residues 51 to 359 or 404 (or 71 to 360) of full-length human PDK1; this may comprise the protein kinase domain of PDK1, as described in Example 2. The PDK1 (or SGK, PKB, PKA or p70 S6 kinase) may also be Myc epitope-tagged or His-tagged, as described in Example 1. The p70 S6 kinase, for example, may have a His tag at its N-terminus and/or may lack the carboxy terminal 104 residues (p70 S6K-T2). The PDK1 or SGK may be a Saccharomyces cerevisiae homologue, for example Pkh1 or Pkh2 (PDK1 homologues) or Ypk1 or Yrk2 (SGK homologues), as described in Casamayor et al (1999) Curr Biol 9, 186-197.

It is particularly preferred, although not essential, that the variant or fragment or derivative or fusion of the PDK1, or the fusion of the variant or fragment or derivative has at least 30% of the enzyme activity of full-length human PDK1 with respect to the phosphorylation of full-length human PKBα on residue Thr308 or SGK1 on residue Thr 256 in either the presence or absence of PtdIns(3,4,5)P₃ or PtdIns(3,4)P₂. It is more preferred if the variant or fragment or derivative or fusion of the said protein kinase, or the fusion of the variant or fragment or derivative has at least 50%, preferably at least 70% and more preferably at least 90% of the enzyme activity of PDK1 with respect to the phosphorylation of PKBα or SGK1. However, it will be appreciated that variants or fusions or derivatives or fragments which are devoid of enzymatic activity may nevertheless be useful, for example by interacting with another polypeptide. Thus, variants or fusions or derivatives or fragments which are devoid of enzymatic activity may be useful in a binding assay, which may be used, for example, in a method of the invention in which modulation of an interaction of a mutated PDK1 of the invention and optionally also PDK1 with a interacting polypeptide or compound, for example an interacting polypeptide comprising the amino acid sequence motif Phe/Tyr-Xaa-Xaa-Phe/Tyr (SEQ ID NO:92), for example Phe/Tyr-Xaa-Xaa-Phe/Tyr-Zaa-Phe/Tyr (SEQ ID NO:93), for example Phe/Tyr-Xaa-Xaa-Phe/Tyr-Asp/Glu-Phe/Tyr (SEQ ID NO:94) or Phe/Tyr-Xaa-Xaa-Phe/Tyr-PhosphoSer/PhosphoThr-Phe/Tyr (SEQ ID NO: 95) is measured.

It is preferred that the variant or fragment or derivative or fusion of the said hydrophobic/phosphate binding pocket-containing protein kinase, or the fusion of the variant or fragment or derivative comprises a hydrophobic pocket and a phosphate binding pocket in the position equivalent to the hydrophobic and phosphate binding pocket of human PDK1, as discussed further below.

Equivalent preferences apply to a variant or fragment or derivative or fusion of the SGK, PKB, p70 S6 kinase, p90 RSK, PKCα, PKCδ, PKCζ or PRK2 (for example), or the fusion of the variant or fragment or derivative, with the substitution in relation to SGK, PKB and p70S6 kinase of the peptide substrate Crosstide (GRPRTSSFAEG, SEQ ID NO:96), or for PKB and SGK of the peptide substrate RPRAATF; the substitution in relation to PKA of the peptide substrate Kemptide (LRRASLG, SEQ ID NO:97); the substitution in relation to PKC isoforms and PRK1/2 of histone H1; and the substitution in relation to MSK1/2 or p90-RSK1/2/3 of CREBtide (EILSRRPSYRK, SEQ ID NO:98).

By “variants” of a polypeptide we include insertions, deletions and substitutions, either conservative or non-conservative. In particular we include variants of the polypeptide where such changes do not substantially alter the activity of the said polypeptide, for example the protein kinase activity of PDK1, as described above.

By “conservative substitutions” is intended combinations such as Gly, Ala; Val, Ile, Leu; Asp, Glu; Asn, Gln; Ser, Thr; Lys, Arg; and Phe, Tyr.

The three-letter amino acid code of the IUPAC-IUB Biochemical Nomenclature Commission is used herein, with the exception of the symbol Zaa (negatively charged amino acid). In particular, Xaa represents any amino acid. It is preferred that Xaa and Zaa represent a naturally occurring amino acid. It is preferred that at least the amino acids corresponding to the consensus sequences defined above are L-amino acids.

It is particularly preferred if the PDK1 (or SGK, PKB, PKA or p70 S6 kinase or other hydrophobic/phosphate binding pocket-containing kinase as defined above) variant has an amino acid sequence which has at least 65% identity with the amino acid sequence of PDK1 referred to above (or the sequence for SGK (including SGK1, 2 and 3), PKB, PKA or p70 S6 kinase, for example, as appropriate, referred to above), more preferably at least 70%, 71%, 72%, 73% or 74%, still more preferably at least 75%, yet still more preferably at least 80%, in further preference at least 85%, in still further preference at least 90% and most preferably at least 95% or 97% identity with the amino acid sequence defined above.

It is still further preferred if the PDK1 (or SGK, PKB, PKA or p70 S6 kinase or other hydrophobic/phosphate binding pocket-containing kinase, as defined above) variant has an amino acid sequence which has at least 65% identity with the amino acid sequence of the catalytic domain, particularly the residues forming the hydrophobic pocket, of PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) in the appropriate sequence referred to above, more preferably at least 70%, 71%, 72%, 73% or 74%, still more preferably at least 75%, yet still more preferably at least 80%, in further preference at least 83 or 85%, in still further preference at least 90% and most preferably at least 95% or 97% identity with the amino acid sequence defined above. It will be appreciated that the catalytic domain of a protein kinase-related polypeptide may be readily identified by a person skilled in the art, for example using sequence comparisons as described below.

The percent sequence identity between two polypeptides may be determined using suitable computer programs, for example the GAP program of the University of Wisconsin Genetic Computing Group and it will be appreciated that percent identity is calculated in relation to polypeptides whose sequence has been aligned optimally.

The alignment may alternatively be carried out using the Clustal W program (Thompson et al (1994) Nucl Acid Res 22, 4673-4680). The parameters used may be as follows:

Fast pairwise alignment parameters: K-tuple(word) size; 1, window size; 5, gap penalty; 3, number of top diagonals; 5. Scoring method: x percent.

Multiple alignment parameters: gap open penalty; 10, gap extension penalty; 0.05.

Scoring matrix: BLOSUM.

It is preferred that the PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) is a polypeptide which consists of the amino acid sequence of the protein kinase PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase as the case may be) sequence referred to above or naturally occurring allelic variants thereof. It is preferred that the naturally occurring allelic variants are mammalian, preferably human, but may alternatively be homologues from parasitic or pathogenic or potentially pathogenic organisms. Examples of such organisms and homologues, and of uses of modulators of such homologues are given in U.S. patent application No. 60/112,114, filed on 14 Dec. 1998, and applications claiming priority therefrom, or in Casamayor et al (1999) Curr Biol 9, 186-197.

It is preferred that the PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) is a polypeptide that is capable of interacting with a polypeptide comprising the amino acid sequence motif Phe/Tyr-Xaa-Xaa-Phe/Tyr (SEQ ID NO:92), preferably Phe-Xaa-Xaa-Phe/Tyr, more preferably Phe-Xaa-Xaa-Phe, still more preferably Phe/Tyr-Xaa-Xaa-Phe/Tyr-Xaa-Phe/Tyr (SEQ ID NO:93) or Phe/Tyr-Xaa-Xaa-Phe/Tyr-COOH, for example the polypeptide PIF or PIFtide, as defined below. Further preferences for the said polypeptide are as given above.

The protein kinase activity of PKB, SGK or p70 S6 kinase that is modulated may be phosphorylation of the underlined residue in a polypeptide with the amino acid sequence Arg-Xaa-Arg-Xaa-Xaa-Ser/Thr (SEQ ID NO:100). The polypeptide may be Glycogen Synthase Kinase 3 (GSK3), 40 S ribosomal subunit S6, BAD, 6-phosphofructo-2-kinase, phosphodiesterase 3b, human caspase 9, endothelial nitric oxide synthase or BRCA1.

A compound identified by a method of the invention may modulate the ability of the protein kinase to phosphorylate different substrates, for example different naturally occurring polypeptides, to different extents. The compound may inhibit the protein kinase activity in relation to one substrate but may increase the protein kinase activity in relation to a second substrate. For example, the protein kinase activity of PDK1 may be modulated to a different extent for PKB when compared with SGK, p70 S6 kinase and/or PKC.

It will be appreciated that the modulatory, for example inhibitory action of a compound found to bind (or inhibit binding of a polypeptide or compound) to the protein kinase may be confirmed by performing an assay of enzymic activity (for example PDK1 and/or PDK2 protein kinase activity) in the presence of the compound.

By “hydrophobic pocket-containing protein kinase having a hydrophobic pocket (PIF binding pocket) in the position equivalent to the hydrophobic pocket of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and/or Leu155 of full-length human PDK1 and further having a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and/or Gln150,” is meant a polypeptide having an amino acid sequence identifiable as that of a protein kinase catalytic domain, and further having a predicted or determined three-dimensional structure that includes a hydrophobic pocket corresponding to the region indicated in Example 1 as the PIF binding pocket, and a pocket corresponding to the region indicated in Example 1 as the phosphate binding pocket. The hydrophobic pocket and phosphate binding pockets in PDK1 do not overlap with the ATP or phosphorylation site binding sites on PDK1.

It is preferred that the protein kinase has identical or conserved residues that are equivalent to Lys 115, Ile118, Ile119, Val124, Val127 and/or Leu 155 of human PDK1, more preferably at least Lys115 and Leu155 of human PDK1, most preferably an identical residue equivalent to Leu155. Thus, for example, the protein kinase may have a Lys residue at the position equivalent to Lys115 of PDK1 and/or a Leu residue at the position equivalent to Leu155 of PDK1. It is preferred that the protein kinase does not have an Ala at the position equivalent to Lys115 and/or a Ser, Asp or Glu at the position equivalent to Leu155 of PDK1.

It is further preferred that the protein kinase has identical or conserved residues that are equivalent to Lys76, Arg131, Thr148 and/or Gln 150 of human PDK1, more preferably at least Lys76 and Gln150 of human PDK1, most preferably an identical residue equivalent to Gln150. FIG. 5B shows an alignment of examples of protein kinases considered to have a phosphate binding pocket at the position equivalent to the said phosphate binding pocket of PDK1. Sequence conservation/preferred residues at the positions identified are discussed further in Example 1.

An amino acid sequence may be identifiable as that of a protein kinase catalytic domain by reference to sequence identity or similarities of three dimensional structure with known protein kinase domains, as known to those skilled in the art.

Protein kinases show a conserved catalytic core, as reviewed in Johnson et al (1996) Cell, 85, 149-158 and Taylor & Radzio-Andzelm (1994) Structure 2, 345-355. This core folds into a small N-terminal lobe largely comprising anti-parallel β-sheet, and a large C-terminal lobe which is mostly α-helical.

A deep cleft at the interface between these lobes is the site of ATP binding, with the phosphate groups near the opening of the cleft.

Protein kinases also show conserved sequences within this catalytic core, and the residue equivalent to a given residue of, for example, PDK1, may be identified by alignment of the sequence of the kinase with that of known kinases in such a way as to maximise the match between the sequences. The alignment may be carried out by visual inspection and/or by the use of suitable computer programs, for example the GAP program of the University of Wisconsin Genetic Computing Group, which will also allow the percent identity of the polypeptides to be calculated. The Align program (Pearson (1994) in: Methods in Molecular Biology, Computer Analysis of Sequence Data, Part II (Griffin, A M and Griffin, H G eds) pp 365-389, Humana Press, Clifton).

The comparison of amino acid sequences or three dimension structure (for example from crystallography or computer modelling based on a known structure) may be carried out using methods well known to the skilled man, for example as described in WO 01/44497.

MAP kinase, MEK1, Cdk2 and Erk2 (for example) are not protein kinases having a hydrophobic pocket in the position equivalent to the hydrophobic (PIF binding) pocket of PDK1. MEK1, Cdk2 and ERK2 may have a larger hydrophobic pocket which interacts with an amino acid sequence motif (which may be Phe-Xaa-Phe-Pro, SEQ ID NO:101) which is not Phe-Xaa-Xaa-Phe (SEQ ID NO:99). Thus, these protein kinases do not have a hydrophobic pocket in the position equivalent to the said hydrophobic (PIF-binding) pocket of PDK1.

A further aspect of the invention provides a mutated protein kinase, wherein the protein kinase before mutation has a hydrophobic pocket in the position equivalent to the hydrophobic pocket (PIF-binding pocket) of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and/or Leu155 of full-length human PDK1 and further has a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and/or Gln150, and wherein one or more residues equivalent to Ile118, Val124, Val127, Lys76 or Thr148 forming part of the hydrophobic pocket or phosphate binding pocket of the protein kinase is mutated. It is preferred that the said protein kinase is PDK1. The said protein kinase may alternatively be, for example, SGK, PKB or p70 S6 kinase. It is particularly preferred that the residue at the position equivalent to residue Lys76 of PDK1 is mutated to an Ala. The mutated protein kinase may be useful in determining whether a polypeptide or compound interacts with the hydrophobic (PIF binding) pocket or phosphate binding pocket of the unmutated protein kinase. For example, the abilities of a compound (including polypeptide) to bind to the mutated and unmutated protein kinase, or to modulate the activity of the protein kinase towards one or more substrates of the protein kinase, may be measured and compared.

The mutated protein kinase may alternatively or in addition be mutated at a residue forming part of the “hydroxyl-pocket” discussed in Example 6, for example the residue equivalent to Thr222 and/or Gln 220 of full length human PDK1. These residues are involved in the binding of the UCN-01 7-hydroxyl group.

A further aspect of the invention provides a polynucleotide encoding a mutated protein kinase of the invention. A still further aspect of the invention provides a recombinant polynucleotide suitable for expressing a mutated protein kinase of the invention. A yet further aspect of the invention provides a host cell comprising a polynucleotide of the invention.

A further aspect of the invention provides a method of making a mutated protein kinase of the invention, the method comprising culturing a host cell of the invention which expresses said mutated protein kinase and isolating said mutated protein kinase.

A further aspect of the invention provides a mutated protein kinase obtainable by the above method.

Examples of these aspects of the invention are provided in Example 1, and may be prepared using routine methods by those skilled in the art, for example as described in WO 00/35946.

For example, the above mutated protein kinase may be made by methods well known in the art and as described below and in Example 1 or 2, for example using molecular biology methods or automated chemical peptide synthesis methods.

It will be appreciated that peptidomimetic compounds may also be useful. Thus, by “polypeptide” or “peptide” we include not only molecules in which amino acid residues are joined by peptide (—CO—NH—) linkages but also molecules in which the peptide bond is reversed. Such retro-inverso peptidomimetics may be made using methods known in the art, for example such as those described in Mézière et al (1997) J. Immunol. 159, 3230-3237, incorporated herein by reference. This approach involves making pseudopeptides containing changes involving the backbone, and not the orientation of side chains. Retro-inverse peptides, which contain NH—CO bonds instead of CO—NH peptide bonds, are much more resistant to proteolysis.

Similarly, the peptide bond may be dispensed with altogether provided that an appropriate linker moiety which retains the spacing between the Ca atoms of the amino acid residues is used; it is particularly preferred if the linker moiety has substantially the same charge distribution and substantially the same planarity as a peptide bond.

It will be appreciated that the peptide may conveniently be blocked at its N- or C-terminus so as to help reduce susceptibility to exoproteolytic digestion.

The invention further provides a method of identifying a compound that modulates the protein kinase activity of a protein kinase having a hydrophobic pocket and phosphate binding pocket in the positions equivalent to the hydrophobic (PIF binding) pocket and phosphate binding pocket of PDK1, as defined above (for example PDK1), comprising the step of determining the effect of the compound on the protein kinase activity of, or ability of the compound to bind to the said mutated protein kinase of the invention.

The method may further comprise determining the effect of the compound on the protein kinase activity of, or ability of the compound to bind to, the protein kinase (for example PDK1) which is not mutated at the said residue. When the protein kinase is PDK1, it may lack a functional PH domain (ie it may lack a PH domain capable of binding a phosphoinositide).

It will be appreciated that the protein kinase or mutated protein kinase may be a fusion protein comprising a tag, for example to aid purification, for example a GST tag, as described in Example 1.

The capability of the said PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) polypeptide with regard to interacting with or binding to a polypeptide or other compound may be measured by any method of detecting/measuring a protein/protein interaction or other compound/protein interaction, as discussed further below. Suitable methods include methods analagous to those described in Example 1, as well as other methods, for example yeast two-hybrid interactions, co-purification, ELISA, co-immunoprecipitation and surface plasmon resonance methods. Thus, the said PDK1 (or SGK, PKB, PKA or p70 S6 kinase) may be considered capable of binding to or interacting with a polypeptide or other compound If an interaction may be detected between the said PDK1 polypeptide and the said interacting polypeptide by ELISA, co-immunoprecipitation or surface plasmon resonance methods or by a yeast two-hybrid interaction or copurification method, for example as described in Example 1.

It is preferred that the interaction can be detected using a surface plasmon resonance method, as described in Example 1. The interacting polypeptide (for example a polypeptide comprising a phosphorylated “hydrophobic motif”, for example 56K-pHM; see example 1) may be immobilised on the test surface, for example it can be coupled through amino groups to a Sensor Chip CM5™, according to the manufacturer's instructions, or a biotinylated polypeptide can be bound to an avidin coated Sensor Chip SA. The protein kinase (at concentrations between, for example 0 and between 10 μM and 1.0 μM, for example 2 μM) is then injected over the surface and steady state binding determined in each case. From these measurements a K_(d) can be determined. It is preferred that the interaction has a K_(d) of less than 8 μM, more preferably less than 5 μM, 2 μM, 1 μM, 500 nM, 300 nM, 200 nM or 100 nM, for example about 150 nM. Alternatively, a K_(d) can be determined for a polypeptide or other compound in competition with the immobilised polypeptide (or other compound). The protein kinase (for example at a concentration of 0.5 μM) is mixed with free polypeptide (for example, at concentrations between 0 and 3 μM) and the mixture injected over the immobilised polypeptides. The steady state binding is determined in each case, from which the K_(d) of the interaction can be determined using the Cheng-Prescott relationship. Alternatively, the interaction may be expressed in terms of an observed response or relative observed responses, measured in terms of mass of protein bound to the surface, as described in Example 2. For example, the polypeptide may be immobilised by amino coupling to a Sensor Chip CM5 and each protein kinase (for example different mutated protein kinases, as discussed below) for example at a concentration of 1.0 μM or a range of concentrations, injected over the immobilised polypeptide. Alternatively, the polypeptide may be immobilised on a SA Sensor Chip and each protein kinase, for example at a concentration of 40 nM or a range of concentrations injected over the immobilised polypeptide. The steady state response for each protein kinase is determined, for example expressed in Response Units (RU). 1000 RU corresponds to 1 ng/mm² of protein bound to the surface. A response of less than 10 RU may indicate that no interaction has taken place. A response of at least 10 RU may indicate that the immobilised and injected molecules interact with each other.

It will be appreciated that the above methods may be used to determine whether a particular polypeptide or compound interacts with a protein kinase or mutated protein kinase.

The effect of the compound on the rate or degree of phosphorylation of a hydrophobic pocket and/or phosphate binding pocket-dependent substrate may be determined. A compound may be selected that decreases the protein kinase activity of the said protein kinase, for example PDK1, towards a hydrophobic pocket-dependent substrate or a phosphate binding pocket-dependent substrate and does not affect or increases the protein kinase activity towards a hydrophobic pocket or phosphate binding pocket-independent substrate, for example PKB when the kinase is PDK1. An activator of PDK1 may mimic insulin and may be useful in treating diabetes or obesity, and may protect cells from apoptosis.

Compounds that bind specifically to the phosphate binding site may activate PDK1 (or other AGK kinase having a phosphate binding site). Also compounds that bind to the residues forming part of the phosphate binding site might transduce the negative effect and inhibit the kinase activity. A compound interacting with the phosphate binding site of PDK1 may be an activator, but only of a subset of substrates. Some substrates of PDK1 require the interaction with the phosphate binding site, such as S6K and SGK.

To generate a specific molecule that could bind to the phosphate and/or PIF-binding pocket of PDK1 a anti-idiotype strategy using combinatorial RNA libraries could be employed. Previous studies have established that Combinatorial RNA libraries can be used to isolate specific ligands, called aptamers, for virtually any target molecule by a procedure probably best known as SELEX (Ellington, A. D., and Szostak, J. W. (1990) Nature 346, 818-822; Tuerk, C., and Gold, L. (1990) Science 249, 505-510). Using this approach RNA molecules that interact with antibodies raised against PIFtide or peptides that encompass the hydrophobic motif of AGC kinases which are phosphorylated at their hydrophobic motif would be selected (preferably antibodies that are specific for the phosphorylated form ie bind the phosphorylated form but not the non-phosphorylated form). These RNA species then may have the intrinsic conformation to interact with the phosphate binding (and possibly also the PIF-binding) pocket(s) of PDK1. Antibodies to the phosphate binding pocket may be produced. For example, animals could be immunised with wild type PDK1. Serum could then be purified with a column where the resin is coated with wild type PDK1 used for the immunisation. Specific antibodies could then be passed through columns coated with mutant PDK1 molecules differing only in that they have specific mutations in the phosphate binding pocket, such as Arg131, Lys76 or Gln150, for example mutated to Ala. Antibodies that don't bind to this mutant will either be specific antibodies that recognise the specific motifs or antibodies that are sensitive to the conformational changes associated with these mutations. The opposite development could also be performed: antibodies against a mutant PDK1 having a specific mutation(s) in the phosphate binding pocket, such as Arg131, Lys76 or Gln150, for example mutated to Ala, could be produced and the serum further purified through columns coated with wild type PDK1.

Thus, a further aspect of the invention provides an antibody reactive with the phosphate binding pocket of PDK1 or other hydrophobic pocket (PIF binding pocket)-containing protein kinase having a hydrophobic pocket in the position equivalent to the hydrophobic pocket of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and/or Leu155 of full-length human PDK1 and further having a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and/or Gln150. A further aspect of the invention provides an antibody reactive with PDK1 or other phosphate-binding pocket-containing protein kinase as defined above but not with the said protein kinase mutated at the phosphate binding site, or vice versa. A further aspect of the invention provides a method for preparing or selecting an antibody wherein the antibody is prepared or selected against a said protein kinase (for example PDK1) unmutated at the phosphate binding site and a said protein kinase mutated at the phosphate binding site.

By the term “antibody” is included synthetic antibodies and fragments and variants (for example as discussed above) of whole antibodies which retain the antigen binding site. The antibody may be a monoclonal antibody, but may also be a polyclonal antibody preparation, a part or parts thereof (for example an F_(ab) fragment or F(ab)₂) or a synthetic antibody or part thereof. Fab, Fv, ScFv and dAb antibody fragments can all be expressed in and secreted from E. coli, thus allowing the facile production of large amounts of the said fragments. By “ScFv molecules” is meant molecules wherein the V_(H) and V_(L) partner domains are linked via a flexible oligopeptide. IgG class antibodies are preferred.

Suitable monoclonal antibodies to selected antigens may be prepared by known techniques, for example those disclosed in “Monoclonal Antibodies: A manual of techniques”, H. Zola (CRC Press, 1988) and in “Monoclonal Hybridoma Antibodies: techniques and Applications”, JGR Hurrell (CRC Press, 1982), modified as indicated above. Bispecific antibodies may be prepared by cell fusion, by reassociation of monovalent fragments or by chemical cross-linking of whole antibodies. Methods for preparing bispecific antibodies are disclosed in Corvalen et al, (1987) Cancer Immunol. Immunother. 24, 127-132 and 133-137 and 138-143.

A general review of the techniques involved in the synthesis of antibody fragments which retain their specific binding sites is to be found in Winter & Milstein (1991) Nature 349, 293-299.

For example, an antibody that does not bind PDK1 Arg131Ala could be specifically recognising this residue in the phosphate binding site, but could also be recognising specifically the inactive conformation of PDK1, which is stabilised by Arg 131. The opposite development could also be performed: antibodies against a mutant PDK1 Arg131Ala could be produced and the serum further purified through columns coated with wild type PDK1. In this way, antibodies may be prepared that would either not be able to interact with the phosphate binding site Arg 131 but only when a small residue is in its place, or antibodies that are probes for the active conformation of PDK1. These conformational probes could be used in high throughoutput screenings, HTS, in the search of compounds that are capable of modifying the conformation of the given protein kinase. Antibodies could have been produced with previous knowledge to detect active protein kinases by immunising with active protein kinases, but in those cases, the antibodies would have recognised also the phosphorylation events that make a protein kinase be active. In the methodology here described using antibodies, the conformational probes could be easily isolated. Furthermore, antibodies obtained from an active protein kinase (with overall modifications that make it active) could be further purified through a column coated with the inactive protein kinase (keeping the non bound fraction) and then further purified on a column coated with a protein kinase consisting of an activating mutation (such as R131A in the case of PDK1), retaining the specifically bound fraction, which could be an active conformation probe. This type of approach could also allow the development of conformation specific probes by the use of activating or inhibiting mutations.

A further aspect of the invention provides a kit of parts useful in carrying out a method according to the preceding aspect of the invention, comprising (1) a mutated protein kinase of the invention and (2) the protein kinase which is not a mutated said protein kinase as defined above.

The protein structures described herein (for example with the co-ordinates shown in Examples 2, 3 or 4, or structures modelled thereon) may be useful in designing further reagents that may be useful in drug screening assays or characterisation of protein kinase activity or regulation. For example, such structures may be useful in designing mutants that may be useful in FRET-based activities, for example in which surface residues near to binding sites are mutated to cysteines to allow coupling of chromophores. For example, the cysteine residue may be fluorescently-labelled, and a change in fluorescence intensity or frequency may be detected in an assay. Any thiol-reactive fluorophore, for example BADAN (see, for example, Wadum et al Fluorescently labeled bovine acyl-CoA binding protein—an acyl-CoA sensor. Interaction with CoA and acyl-CoA esters and its use in measuring free acyl CoA esters and non-esterified fatty acids (NEFA); Hammarstrom et al (2001) Biophys J 80(6), 2867-2885; Schindel et al (2001) Eur J Biochem 268(3), 800-808), could be used to label the cysteine. An alternative suitable fluorophore is Acrylodan (Richieri et al (1992) J Biol Chem 267(33), 23495-23501).

It will be appreciated that the invention provides screening assays for drugs which may be useful in modulating, for example either enhancing or inhibiting, the protein kinase activity of a protein kinase (for example, the protein kinase activity towards a particular substrate) having a hydrophobic pocket in the position equivalent to the hydrophobic pocket of Protein Kinase A (PKA) that is defined by residues including Lys76, Leu116, Val80 and/or Lys111 of full-length mouse PKA, for example PDK1, SGK, PKB, PKA or p70 S6 kinase, for example the PDK1 or PDK2 activity (as discussed above) of PDK1. The compounds identified in the methods may themselves be useful as a drug or they may represent lead compounds for the design and synthesis of more efficacious compounds.

The compound may be a drug-like compound or lead compound for the development of a drug-like compound for each of the above methods of identifying a compound. It will be appreciated that the said methods may be useful as screening assays in the development of pharmaceutical compounds or drugs, as well known to those skilled in the art.

The term “drug-like compound” is well known to those skilled in the art, and may include the meaning of a compound that has characteristics that may make it suitable for use in medicine, for example as the active ingredient in a medicament. Thus, for example, a drug-like compound may be a molecule that may be synthesised by the techniques of organic chemistry, less preferably by techniques of molecular biology or biochemistry, and is preferably a small molecule, which may be of less than 5000 daltons. A drug-like compound may additionally exhibit features of selective interaction with a particular protein or proteins and be bioavailable and/or able to penetrate cellular membranes, but it will be appreciated that these features are not essential.

The term “lead compound” is similarly well known to those skilled in the art, and may include the meaning that the compound, whilst not itself suitable for use as a drug (for example because it is only weakly potent against its intended target, non-selective in its action, unstable, difficult to synthesise or has poor bioavailability) may provide a starting-point for the design of other compounds that may have more desirable characteristics.

It is appreciated that screening assays which are capable of high throughput operation are particularly preferred. Examples may include cell based assays and protein-protein binding assays. An SPA-based (Scintillation Proximity Assay; Amersham International) system may be used. For example, beads comprising scintillant and a substrate polypeptide or interacting polypeptide may be prepared. The beads may be mixed with a sample comprising ³²P- or ³³P-γ-labelled PDK1 or other protein kinase or mutated protein kinase (as defined above) and with the test compound. Conveniently this is done in a 96-well or 384-well format. The plate is then counted using a suitable scintillation counter, using known parameters for ³²P or ³³P SPA assays. Only ³²P or ³³P that is in proximity to the scintillant, i.e. only that bound to the substrate or interacting polypeptide that is bound to the beads, is detected. Variants of such an assay, for example in which the substrate or interacting polypeptide is immobilised on the scintillant beads via binding to an antibody or antibody fragment, may also be used.

It will be understood that it will be desirable to identify compounds that may modulate the activity of the protein kinase in vivo. Thus it will be understood that reagents and conditions used in the method may be chosen such that the interactions between, for example, the said protein kinase and the interacting polypeptide, are substantially the same as between the human protein kinase and a naturally occurring interacting polypeptide comprising the said amino acid sequence. It will be appreciated that the compound may bind to the protein kinase, or may bind to the interacting polypeptide.

The compounds that are tested in the screening methods of the assay or in other assays in which the ability of a compound to modulate the protein kinase activity of a protein kinase, for example a hydrophobic pocket-containing protein kinase, as defined above, may be measured, may be compounds that have been selected and/or designed (including modified) using molecular modelling techniques, for example using computer techniques.

A further aspect of the invention is a compound identified or identifiable by the above selection/design methods of the invention, for example an RNA molecule or antibody identifiable as defined above.

A still further aspect of the invention is a compound (or polypeptide or polynucleotide) of the invention or identified or identifiable by the above selection/design methods of the invention, for use in medicine. Conditions or diseases in which such compounds, polypeptides or polynucleotides may be useful are indicated below.

The compound (or polypeptide or polynucleotide) may be administered in any suitable way, usually parenterally, for example intravenously, intraperitoneally or intravesically, in standard sterile, non-pyrogenic formulations of diluents and carriers. The compound (or polypeptide or polynucleotide) may also be administered topically, which may be of particular benefit for treatment of surface wounds. The compound (or polypeptide or polynucleotide) may also be administered in a localised manner, for example by injection. The compound may be useful as an antifungal (or other parasitic, pathogenic or potentially parasitic or pathogenic organism) agent.

A further aspect of the invention is the use of a compound (or polypeptide or polynucleotide) as defined above in the manufacture of a medicament for the treatment of a patient in need of modulation of signalling by a protein kinase having a hydrophobic/phosphate binding pocket, as defined above, for example PDK1, SGK, PKB or p70 S6 kinase, for example insulin signalling pathway and/or PDK1/PDK2/SGK/PKB/p70 S6 kinase/PRK2/PKC signalling. The patient may be in need of inhibition of a said hydrophobic/phosphate binding pocket-containing kinase in an infecting organism, for example the patient may have a fungal infection for which treatment is required. The compound may inhibit the infecting organism's (for example fungal) hydrophobic/phosphate binding pocket-containing protein kinase, but may not inhibit the patient's equivalent hydrophobic/phosphate binding pocket-containing protein kinase.

A further aspect of the invention is a method of treating a patient in need of modulation of signalling by a protein kinase having a hydrophobic/phosphate binding pocket as defined above, for example PDK1, SGK, PKB or p70 S6 kinase, for example insulin signalling pathway and/or PDK1/PDK2/SGK/PKB/p70 S6 kinase/PRK2/PKC signalling, wherein the patient is administered an effective amount of a compound (or polypeptide or polynucleotide) as defined above.

A compound that is capable of reducing the activity of PKC, for example PKCβ, PRK1 or 2, PDK1 (ie the PDK1 and/or the PDK2 activity), PKB, SGK or p70 S6 kinase may be useful in treating cancer. PDK1, for example via PKB and/or SGK, may be capable of providing a survival signal that protects cells from apoptosis induced in a variety of ways (reviewed in Cross et al (1995) Nature 378, 785-789 and Alessi & Cohen (1998) Curr. Opin. Genetics. Develop. 8, 55-62). Thus, such compounds may aid apoptosis. Reduction of the activity of PDK1, PKB, SGK and/or p70 S6 kinase may promote apoptosis and may therefore be useful in treating cancer. Conditions in which aiding apoptosis may be of benefit may also include resolution of inflammation.

A compound is capable of increasing the activity of PDK1, PKB, SGK or p70 S6 kinase may be useful in treating diabetes or obesity, or may be useful in inhibiting apoptosis. Increased activity of PDK1, PKB, SGK or p70 S6 kinase may lead to increased levels of leptin, as discussed above, which may lead to weight loss; thus such compounds may lead to weight loss. For example, such compounds may suppress apoptosis, which may aid cell survival during or following cell damaging processes. It is believed that such compounds are useful in treating disease in which apoptosis is involved. Examples of such diseases include, but are not limited to, mechanical (including heat) tissue injury or ischaemic disease, for example stroke and myocardial infarction, neural injury and myocardial infarction. Thus the patient in need of modulation of the activity of PDK1, PKB, SGK or p70 S6 kinase may be a patient with cancer or with diabetes, or a patient in need of inhibition of apoptosis, for example a patient suffering from tissue injury or ischaemic injury, including stroke.

Thus, a further aspect of the invention provides a method of treating a patient with an ischaemic disease the method comprising administering to the patient an effective amount of a compound identified or identifiable by the screening methods of the invention.

A still further invention provides a use of a compound identifiable by the screening methods of the invention in the manufacture of a medicament for treating an ischaemic disease in a patient.

Thus, a further aspect of the invention provides a method of treating a patient with an ischaemic disease the method comprising administering to the patient an effective amount of a compound identifiable by the screening methods of the invention.

If the patient is a patient in need of promotion of apoptosis, for example a patient with cancer, it is preferred that the compound of the invention that is used in the preparation of the medicament is capable of reducing the activity of PDK1, PKB, SGK or p70 S6 kinase. If the patient is a patient with diabetes or a patient in need of inhibition of apoptosis, for example a patient with ischaemic disease, it is preferred that the compound of the invention that is used in the preparation of the medicament is capable of increasing the activity of PDK1, PKB, SGK or p70 S6 kinase.

All documents referred to herein are hereby incorporated by reference.

The invention is now described in more detail by reference to the following, non-limiting, Figures and Examples.

Figure Legends

1. Overview of the PDK1 Structure.

The PDK1 kinase domain backbone is shown in a ribbon representation, with the secondary structure elements for residues 74-163 in the lower half of the Figure and for residues 164-358 in the upper part of the Figure. Helix αG, encompassing residues 287-295 (which makes a crystal contact to a symmetry related PDK1 molecule, FIG. 2), is at the bottom right of the Figure. Key residues discussed in the text are shown as a sticks model. ATP is shown as a sticks model. A simulated annealing |Fo−|Fc′, φ calc map is shown in black, contoured at 3σ. The phosphoserine and the sulphate discussed in the text are also shown.

2. The PIF-Pocket

A. A surface representation of the putative PIF binding pocket is shown and compared to the pocket interacting with the C-terminal FXXF (SEQ ID NO: 1) motif in PKA. For PDK1, the αG helix of a symmetry-related molecule is shown as a ribbon, in PKA the C-terminus is also shown as a ribbon. Aromatic amino acids buried in the pocket are shown as sticks; further side chains interacting with the pocket are also shown as sticks. Helix αC is also shown as a ribbon in both PDK1 and PKA (at bottom of images). In PDK1, the ordered sulphate ion and basic residues interacting with it are also shown.

B. A stereo image of the residues lining the PIF-pocket is shown. The PDK1 backbone is shown as a grey ribbon. Side chains are shown as sticks. Hydrogen bonds to the sulphate ion are shown as black dotted lines.

3. Structure-Based Sequence Alignment

The sequences of PKA (SEQ ID NO: 103) and PDK1 (SEQ ID NO:102) are aligned according to a structural superposition performed in WHAT IF [Vriend, 1990]. Sequence numbering is according to PDK1. 13-strands (arrows) and α-helices (bars) are shown for the PDK1 structure according to a DSSP [Kabsch and Sander, 1983] secondary structure assignment, and labelled consistent with the secondary structure element names proposed for PKA [Taylor and Radzioandzelm, 1994]. Residues lining the PIF-pocket are indicated with a black dot. Residues hydrogen bonding the sulphate ion are indicated by arrows. The PDK1 residues equivalent to Ser53 and Gly186 in PKA, are labelled with an asterisk.

4. PDK1 Binding & Activation Studies

Binding and activation of wild type and mutant forms of PDK1 to a phosphopeptide derived from the hydrophobic motif of S6K1. The binding of the wild type (wt) PDK1 and indicated mutants to a phosphopeptide comprising the hydrophobic motif of S6K1 (S6K-pHM: SESANQVFLGFT*YVAPSV, where T* indicates phospho-threonine, SEQ ID NO:104) was analysed by surface plasmon resonance as described in the Materials and Methods.

A. The sensor chip SA was coated with 12RUs of the biotinylated S6K-pHM peptide and the binding was analysed following injection of 270 nM wild type PDK1, PDK1 [T148A] and PDK1 [K76A]. No detectable binding to S6K-pHM was observed using PDK1 [R131A] or PDK1 [Q150] (data not shown).

B. As in A. except that binding was analysed over a range of PDK1 concentrations (2-2150 nM). The response level at the steady state binding is plotted versus the log of the PDK1 concentration. The estimated Kd was obtained by fitting the data to a sigmoid curve using Kaleidagraph software. Kd for wild type PDK1 was 642-131 nM, PDK1 [T148A] was 64-7 nM and PDK1 [K76A] was 1744-167 nM. No detectable binding of PDK1 to the non-phosphorylated S6K-HM peptide (SESANQVFLGFTYVAPSV, SEQ ID NO:105) was detected with wild type PDK1 or any of the mutants (data not shown).

C. Activation of the indicated forms of PDK1 by 56K-pHM and S6K-HM. PDK1 activity was measured using the peptide substrate (T308tide) in the presence of the indicated concentrations of 56K-pHM (closed circles) and S6K-HM (open circles) as described in the methods. Assays were performed in triplicate and similar results obtained in 2 separate experiments. The results are the average—SD for a single experiment.

5. Interactions of Regulatory Phosphates with the αC Helix

A. The PDK1 backbone is shown as a ribbon, with helix a C in the centre of the view. Key residues are shown as sticks. The sulphate ion and the phosphate on the activation loop are also shown. A sticks model of ATP is shown. Hydrogen bonds are shown as black dotted lines.

B. Alignment of the amino acid sequence forming part of the phosphate pocket on PDK1 with the equivalent region of the indicated AGC kinases. Identical residues are denoted by white letters on a black background and similar residues by gray boxes. Arrows indicate the residues corresponding to Lys 76, Arg131, Thr148 and Gln150 of PDK1 (SEQ ID NOs:12 and 144). The aligned amino acid sequences are as follows: PKBα (SEQ ID NOs: 13 and 145), S6K1 (SEQ ID NOs: 14 and 146), SGK1 (SEQ ID NOs: 15 and 147), and Rsk1 (SEQ ID NOs: 16 and 148).

6. Essential Dynamics

A. Projection of all available PKA crystal structures (labelled dots) and the PDK1 structure (diamond) onto the first two eigenvectors (i.e. the ones with the two largest eigenvalues) calculated from the PKA structures.

B. Graphic representation of the motion along the first eigenvector, generated by projecting two structures at −4 nm (black) and +4 nm (grey).

7. Alignment of AGC Protein Kinase Family Members.

The aligned amino acid sequences and their respective corresponding sequence identifier are as follows:

P70S6Kalpha (SEQ ID NO: 17), P70S6 Kbeta (SEQ ID NO: 18), P90RSK1 (SEQ ID NO: 19), P90RSK2 (SEQ ID NO: 20), P90RSK3 (SEQ ID NO: 21), MSK1 (SEQ ID NO: 22), MSK2 (SEQ ID NO: 23), PKBalpha (SEQ ID NO: 24), PKBbeta (SEQ ID NO: 25), PKBgamma (SEQ ID NO: 26), PRK1 (SEQ ID NO: 27), PRK2 (SEQ ID NO: 28), SGK1 (SEQ ID NO: 29), SGK3 (SEQ ID NO: 30), SGK2 (SEQ ID NO: 31), PKCbeta (SEQ ID NO: 32), PKCbetaII (SEQ ID NO: 33), PKCalpha (SEQ ID NO: 34), PKCgamma (SEQ ID NO: 35), PKCzeta (SEQ ID NO: 36), PKCiota (SEQ ID NO: 37), PKCdelta (SEQ ID NO: 38), PKAgamma (SEQ ID NO: 39), and PDK1 (SEQ ID NO: 40).

8. Staurosporine and UCN-01 Electron Density.

The staurosporine and UCN-01 molecules are shown in a stick representation. Hydrogen bonding atoms (Table 4) are labelled according to [49]. The unbiased |F_(o)|−|F_(c)|, φ_(calc) maps are contoured at 2.5σ.

9. Details of the Inhibitor Binding Sites.

The bridging water molecule is shown as a sphere. Hydrogen bonds are indicated by black dotted lines. Labelled residues hydrogen-bond the inhibitor molecules.

Example 1 High Resolution Crystal Structure of the Human PDK1 Catalytic Domain Defines the Regulatory Phosphopeptide Docking Site

The 3-Phosphoinositide Dependent Protein Kinase-1 (PDK1) plays a key role in insulin/growth factor induced signalling pathways through phosphorylation of downstream AGC-kinases such as Protein Kinase B/Akt and p70 ribosomal S6 kinase (S6K1). Here we describe the 2.0 Å crystal structure of the PDK1 kinase domain in complex with ATP. The structure defines the hydrophobic pocket termed the ‘PIF-pocket’ which plays a key role in mediating the interaction and phosphorylation of certain substrates such as S6K1. In the PDK1 structure, this pocket is occupied by an extensive crystallographic contact with another molecule of PDK1, reminiscent of the interaction of Protein Kinase A with the hydrophobic motif at its C-terminus. Previous studies have shown that phosphorylation of S6K1 at its C-terminal PIF-pocket-interacting motif, promotes the binding of S6K1 with PDK1, suggesting that there may be a phosphate docking site located nearby the PIF-pocket. Interestingly, close to the PIF-pocket on the PDK1 structure, there is an ordered sulphate ion, interacting tightly with four surrounding side chains. The roles of these residues were investigated through a combination of site directed mutagenesis and kinetic studies, the results of which suggest that this region of PDK1 does indeed represent a phosphate dependent docking site. An analogous phosphate binding regulatory motif may participate in the activation of other AGC kinases.

Results & Discussion

Overall Structure

The structure of the catalytic domain of PDK1 was solved by molecular replacement and refined to an R-factor of 0.19 (Rfree=0.22). PDK1 assumes the classic bilobal kinase fold (FIG. 1) and is similar to the only other AGC kinase structure solved, that of PKA (RMSD of 1.0 Å on C a atoms with PDB entry 1STC [Prade et al., 1997]). The form of PDK1 that was crystallized comprised residues 51 to 359. The tip of the activation loop (residues 233-236) is disordered, as observed in other kinase structures [Johnson et al., 1996]. The N-terminus (residue 51-70), which is pointing into a large void generated by the crystallographic symmetry, is also disordered. In contrast, the N-terminal extension to the kinase domain of PKA assumes an amphipathic α-helix (termed αA-helix), and packs against the kinase core [Knighton et al., 1991]. The cluster of hydrophobic residues that mediates this interaction in PKA is not present in PDK1, suggesting that the N-terminus of PDK1 could have a different function from that of PKA. Interestingly, it has recently been shown that the N-terminus of PDK1 (residues 1-50) interacts with Ral guanine nucleotide exchange factors [Tian et al., 2002]. Thus, this region may assume a unique conformation in PDK1, which is not defined by the structure described here.

PDK1 was crystallised in the presence of ATP but in the absence of any divalent cations. In the early stages of the refinement well-defined density for the entire ATP molecule could be observed. ATP adopts a different conformation to that observed in other kinase-ATP complexes (FIG. 1). Perhaps due to the absence of divalent cations, the generally observed kink between the β and γ phosphate caused by the interaction with such an ion, is not seen in the PDK1 structure.

It is known that PDK1 can phosphorylate itself on residue Ser 241 in the activation loop and that this phosphorylation is required for PDK1 activity [Alessi et al., 1997]. Indeed, we observed density for a phosphate attached to this residue (FIG. 1), and extensive interactions are observed between this phosphoserine and residues from the C-terminal lobe and αC-helix (FIG. 1). The interaction between Ser241 and the C-terminal lobe is similar to the equivalent interactions in PKA but as discussed below the binding to the αC-helix differs.

The PIF-Pocket

As outlined in the introduction, PDK1 was postulated to possess a pocket (the ‘PIF-pocket’) in the small lobe of its catalytic domain, required for the binding of PDK1 to the hydrophobic motif of its substrates [Biondi et al., 2000]. The PDK1 structure described here indeed reveals such a pocket, and shows that it lies in a location similar to the FXXF (SEQ ID NO:1)-binding pocket in PKA (FIG. 2). PDK1 residues Lys115, Ile118, Ile119 on the αB helix (FIG. 2), Val124, Val127 on the αC helix and Leu155 on β-sheet 5 form an approximately 5 Å deep pocket. Previous work has shown that mutation of Leu 155 to Glu abolishes the ability of PDK1 to interact with a peptide that encompasses the hydrophobic motif of PRK2 (PIFtide) [Biondi et al., 2000] as well as with S6K1, SGK1, PKCζ and PRK2 [Balendran et al., 2000, Biondi et al., 2000]. In addition, mutation of Lys115, Ile119, Glu150, and Leu155 to alanine, reduced the affinity of PDK1 for PIFtide approximately 10-fold, but did not affect the ability to phosphorylate and activate S6K1 and SGK1 [Biondi et al., 2001]. These results are in agreement with the crystal structure of the PIF-pocket, since Leu155 is located at the center and the other residues line the wall of the pocket (FIG. 2). Interestingly, in our structure, the PIF-pocket is occupied by helix αG of a symmetry related molecule (FIG. 2). Tyr288 and Phe291 make hydrophobic contacts in this pocket with almost all pocket-lining residues, remarkably reminiscent of the interactions of the phenylalanines in the FXXF motif in PKA and their hydrophobic docking site in the equivalent region of the kinase domain (FIG. 2). In addition, residues Glu287, Gln292, Ile295 and Lys296 on the symmetry related loop also form contacts with residues lining the PIF-pocket. In total, 244² Å of accessible surface is buried by this contact, suggesting this is a tight interaction. However, the significance of this interaction is not clear as an oligomerisation event for PDK1 has not been demonstrated in solution previously. Indeed both the isolated catalytic domain of PDK1 that was crystallised and full length PDK1 migrate in gel filtration chromatography as apparent monomeric species (data not shown).

The Phosphate Pocket

As outlined in the introduction, substrates of PDK1, such as S6K1, interact with the PIF-pocket of PDK1 with higher affinity when they are phosphorylated at their hydrophobic motif. This suggested that a regulatory phosphate binding site may be located close to the PIF-pocket. During refinement of the PDK1 structure, it became clear that next to the PIF-pocket another small pocket was present, occupied by a tetrahedral oxy-anion (FIG. 2). As 2.0 M of sulphate was present in the crystallisation conditions, this was assigned as a sulphate ion. The ion interacts with four residues lining the pocket, namely Lys76, Arg131, Thr148 and Gln150.

Because of its close proximity to the PIF-pocket (approximately 5A) it is possible that this sulphate-occupied pocket could represent the binding site for the phosphate on the phosphopeptide. To investigate this further, we mutated Lys76, Arg131, Thr148 and Gln150 to Ala, in order to verify the contribution of each of these residues in enabling PDK1 to interact with a peptide encompassing the hydrophobic motif of S6K1, in which the residue equivalent to Thr412 was phosphorylated (termed S6K-pHM). A quantitative surface plasmon resonance based binding assay (FIG. 4A) showed that wild type PDK1 interacted with S6K-pHM, with a Kd of 0.6 μM with S6K-pHM but not detectably to the non-phosphorylated form of this peptide (S6K-HM). The PDK1[R131A] and PDK1[Q150A] mutants did not detectably interact with S6K-pHM in this assay (FIG. 4B), confirming that the interactions these residues make in the PDK1 structure are of key importance. The PDK1 [K76A] mutant interacted with 3-fold lower affinity (Kd 1.7 μM) with S6K-pHM. The PDK1[T148A] mutant however possessed about 10-fold higher (Kd 0.06 μM) affinity for S6K-pHM than wild type PDK1. Moreover, the dissociation of PDK1[T148A] from S6K-pHM is markedly slower than that of wild type PDK1 or PDK1[K76A] (FIG. 4A). These findings are unexpected as Thr148 is within hydrogen bonding distance of the sulphate (FIG. 2), but indicate that this residue may play a role in enabling the dissociation of PDK1 from S6K-pHM.

The binding of PDK1 to PIFtide stimulates up to 4-fold the rate at which PDK1 phosphorylates a small peptide that encompasses the activation loop motif of PKB (termed T308tide) [Biondi et al., 2000], indicating that occupancy of the PIF-pocket of PDK1 activates the enzyme. Similarly, the binding of a phosphopeptide corresponding to the hydrophobic motif of RSK stimulated PDK1 activity 6-fold [Frodin et al., 2000]. We have now also found that the binding of 56K-pHM to wild type PDK1 induces a maximal 5-fold activation, with a half maximal activation occurring at a concentration of approximately 50 μM S6K-pHM (FIG. 4C). We next assayed the specific activities of PDK1 [K76A], PDK1[R131A], PDK1[T148A] and PDK1[Q150A] mutants in the absence and presence of increasing concentrations of S6K-pHM (FIG. 4C). The PDK1[K76A] possessed the same specific activity towards T308tide in the absence of S6K-pHM as wild type PDK1, but an approximately 3-fold higher concentration of S6K-pHM was required to half maximally activate PDK1[K76A], consistent with the reduced affinity of this form of PDK1 for S6K-pHM (FIG. 4A,B). The PDK1[R131A] mutant possessed a 3-fold higher specific activity towards Thr308tide in the absence of S6K-pHM (FIG. 4C), as has been observed previously with certain other PIF-pocket mutants of PDK1(PDK1[K115A] and PDK1[L155E]) [Biondi et al., 2000]. However, in accordance with the inability of PDK1[R131A] to bind S6K-pHM in the Biacore assay (FIG. 4B), it was not significantly activated by concentrations of S6K-pHM below 0.1 mM and its activity was only moderately further increased by the addition of high concentrations (0.3 and 1 mM) of S6K-pHM (FIG. 4C). The activity of a mutant of PDK1 in which both Lys76 and Arg131 were changed to Ala was activated even less significantly by these high concentrations of S6K-pHM. The PDK1[T148A] and PDK1[Q150A] mutants possessed similar specific activity towards T308tide as wild type PDK1 in the absence of S6K-pHM. The PDK1[T148A] mutant was activated similarly as wild type PDK1 by S6K-pHM and consistent with the inability of PDK1[Q150A] to interact with S6K-pHM, this mutant of PDK1 was not significantly activated by concentrations of S6K-pHM below 0.1 mM but at 0.3 and 1 mM peptide a 2-3 fold activation was observed (FIG. 4).

At very high peptide concentrations (0.3-1 mM) the non-phosphorylated S6K-HM peptide induced a small (<2-fold) activation of PDK1 (FIG. 4C). Interestingly, despite the PDK1 [K76A] and PDK1[R131A] mutants being markedly less able to interact with the phosphorylated S6K-pHM peptide, than wild type PDK1, high concentrations of the S6K-HM peptide activated PDK1[K76A] and PDK1[R131A] to a similar extent as wild type PDK1, indicating that the ability of these mutants to interact weakly with the S6K-HM peptide was not affected.

We evaluated the sequence conservation in the phosphate pocket of the insulin/growth factor-activated AGC family kinases (PKBα, S6K1, SGK1 and RSK1). Sequence alignments indicate that this pocket is conserved amongst these kinases (FIG. 5A). The most conserved residue is Gln150 which is found in all of these AGC kinases and the residue equivalent to Lys76 is always a basic residue (FIG. 5A). Arg131 is conserved in S6K1, SGK1 and RSK1 but not in PKBα, or PKBβ or PKBγ, where it is an Asn or Ser. Thr148 is conserved in PKBα and SGK1 but is an Ala in S6K1 and RSK1. Interestingly, we have found the Thr 148Ala mutation in PDK1 did not disrupt the phosphate pocket (FIG. 4). As PKBα, S6K1, SGK1 and RSK1 require to be phosphorylated at their hydrophobic motif to be maximally activated, it is tempting to speculate that the C-terminal hydrophobic motifs of these enzymes, when phosphorylated, bind to their own PIF/phosphate pockets, thereby generating a network of interactions similar to that of PDK1. In support of this, PKBα, S6K1, SGK1 and RSK1 also require phosphorylation of their activation loop at the position equivalent to Ser241 for activity. Consistent with PKA not possessing a phosphate pocket, Lys76 and Gln150 are not conserved in PKA (FIG. 3), and indeed such a pocket is not observed in the PKA structure (FIG. 2).

The αC Helix

The PDK1 structure shows that, as in other protein kinases [Johnson et al., 2001, Husen and Kuriyan, 2002], the αC helix (residues 124-136) is a key signal integration motif in the kinase core. One turn of the PDK1 αC helix (residues 129-131, FIGS. 3, 5) links together the N-terminal lobe, the C-terminal lobe and the active site. Arg129 points towards the activation loop and forms two hydrogen bonds with the phosphorylated Ser241, whereas Arg131 forms two hydrogen bonds with the sulphate in the phosphate pocket (FIG. 5). Glu130 coordinates Lys111 which forms a hydrogen bond with the α-phosphate of the bound ATP. This interaction is conserved in all protein kinases and shown to be crucial for activation [Johnson et al., 2001, Husen and Kuriyan, 2002]. An additional residue, His126, forms a third hydrogen bond with the phosphorylated Ser241. Val124 and Val127 on the αC helix are involved in formation of the PIF-pocket (FIG. 5).

The αC helix provides a structural link between the putative phosphopeptide binding pocket and the phosphoserine in the activation loop. The fact that R131A has higher basal activity than wild type PDK1 may indicate that this residue plays tuning role in the PDK1 structure, not only participating in the activation of PDK1 in the presence of a phosphate ion, but also on keeping the equilibrium of the enzyme towards an inactive conformation in the absence of S6K-pHM. To our knowledge this is the first report of a kinase structure in which the αC helix is positioned by 2 regulatory phosphate binding sites on either side of the helix (FIG. 5). This provides a possible sensor-mechanism for linking the phosphorylation-state of the activation loop and the phosphopeptide binding event in the PIF-pocket to PDK1 activity.

Activation State

All structures of PKA solved to date show a phosphorylated T-loop and are therefore assumed to be in an active state. In addition to the unphosphorylated versus phosphorylated states of PKA, there appear to be two main conformational states possible for the latter [Zheng et al., 1993, Johnson et al., 2001]. In the active, closed conformation, all residues are positioned to facilitate phosphoryl transfer. In contrast, the inactive, open conformation is seen in absence of a nucleotide, and differs from the closed conformation by conformational changes of the N-terminal and C-terminal domains with respect to each other. In addition, three ‘intermediate’ structures were described from PKA, having either adenosine (PDB entry 1BKX [Narayana et al., 1997]) or the inhibitors staurosporine (PDB entry 1STC [Prade et al., 1997]) and balanol (PDB entry 1BX6 [Narayana et al., 1999]) in the ATP-binding site. Taylor and colleagues have described a method to distinguish between the active and inactive conformations, based on three distances: His87-pThr197 (αC helix positioning), Ser53-Gly186 (opening of the glycine-rich loop) and Glu170-Tyr330 (C-terminal tail distance to active site) [Johnson et al., 2001]. In PDK1, only one of these distances, the opening state of the glycine rich loop, can be measured due to sequence conservation (FIG. 3). This distance is 12.4 Å, similar to a PKA intermediate conformation (this distance in PKA is 14.2 Å for the open, 11.8 Å for intermediate and 10.0 Å for the closed conformation [Johnson et al., 2001]). To allow a more direct comparison of the PDK1 structure with the available PKA structures, we have analysed the conformational state of PDK1 in detail using a novel approach, which involves a principal component analysis (also called “essential dynamics” [Amadei et al., 1993]) of the crystallographic coordinates. In short, this involves the construction of a covariance matrix containing the correlations between atomic shifts (with respect to an average structure) in the ensemble of all available PKA crystal structures. Diagonalisation of this matrix gives eigenvector/eigenvalue sets which describe concerted shifts of atoms (eigenvectors) together with the corresponding mean square fluctuation of the structures (eigenvalues). This approach allows a condensed description of PKA conformational states using only a few degrees of freedom, as shown previously for a range of other proteins [van Aalten et al., 1997, van Aalten et al., 2000, deGroot et al., 1998]. Diagonalisation of a covariance matrix built from the backbone atoms of residues 37-196, 198-283 and 286-305 results in a set of eigenvectors that describe concerted motions of the PKA backbone. In FIG. 6A, all PKA structures are projected on a subspace spanned by the first two eigenvectors (i.e. those with the two largest eigenvalues). It appears that the PKA structures cluster in three main areas along the first eigenvector. On the left of the average structure (which by definition has a projection of 0.0 on all eigenvectors) are the structures that are known to be in the “open” conformation (FIG. 6A). Around the average structure lie the structures that have been shown to be in an “intermediate” conformation (complexes with the inhibitors staurosporine, balanol and adenosine). More to the right of the average structure are the PKA structures that are known to be in the “closed” conformation. Thus, we have captured the conformational state of PKA in a single variable, the translation along the first eigenvector. This is further clarified by investigation of the atomic shifts described by this eigenvector in Cartesian space (FIG. 6B). A hinge-bending motion is observed between the N-terminal and C-terminal lobes, opening and closing the active site. It is now possible directly to compare the PDK1 conformational state by projecting the structure (backbone atoms only) onto the PKA eigenvectors. FIG. 6A shows that the conformation of PDK1 is close to the PKA structures that are in an “intermediate” conformation, consistent with the other structural analyses described above.

Conclusions

We have reported the structure of the PDK1 catalytic domain, which, although similar to PKA, has revealed important features that increase our understanding of the mechanism by which PDK1 is regulated. The structure, together with mutational analyses, defines a phosphopeptide binding pocket, consisting of a separate hydrophobic PIF-pocket and a phosphate binding site, which mediates the interaction of PDK1 with the phosphorylated hydrophobic motif of S6K. This is consistent with the previous hypothesis that phosphorylation of S6K and SGK [Biondi et al., 2001] as well as RSK [Frodin et al., 2000] at their FXXFS/T hydrophobic motif (SEQ ID NO:2) is the trigger for their interaction and phosphorylation by PDK1. In this mechanism the PIF-pocket would physiologically only interact with the Phe residues when the Ser/Thr residue is phosphorylated. Furthermore, as the phosphate pocket is conserved in other AGC kinases, the structural features and network of interaction of the phosphate pocket with the αC-helix on PDK1, could provide insight into the mode of activation of other AGC kinases.

EXPERIMENTAL PROCEDURES Materials

Mammalian and Insect cells culture reagents were from Life Technologies. Sensor Chips SA were from BiaCore AB. Glutathione Sepharose, as well as pre-packed HiTrap Q HP and Hiload Superdex 200 prep grade columns were from Amersham Biosciences. Dialysis cassettes were from the Slide-A-Lyzer series (Pierce). Ni-NTA Agarose was from Qiagen. Disposable ultrafiltration devices (polyethersulfone membranes) were from Vivascience. Crystallisation research tools (primary screens, additive screens and crystallisation plates) were from Hampton Research. Peptides were synthesised by Dr G. Blomberg (University of Bristol, UK).

General Methods

Molecular biology techniques were performed using standard protocols. Site directed mutagenesis was performed using a QuickChange kit (Stratagene) following instructions provided by the manufacturer. DNA constructs used for transfection were purified from bacteria using Qiagen plasmid Mega kit according to the manufacturer's protocol, and their sequence verified. Human kidney embryonic 293 cells were cultured on 10 cm diameter dishes in Dulbecco's modified Eagle's medium containing 10% foetal bovine serum.

Buffers

Low Salt Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl; High Salt Buffer: 25 mM Tris-HCl pH 7.5, 500 mM NaCl. Lysis Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl 0.07% β-mercaptoethanol, 1 mM Benzamidine, and 20 μg/ml PMSF. Buffer A: 50 mM Tris-HCl pH 7.5, 1 mM EGTA, 1 mM EDTA, 1% (by mass) Triton-X 100, 1 mM sodium orthovanadate, 50 mM sodium fluoride, 5 mM sodium pyrophosphate, 0.27 M sucrose, 1 μM microcystin-LR, 0.1% (by vol)-mercaptoethanol and “complete” proteinase inhibitor cocktail (one tablet per 50 ml, Roche). Buffer B: 50 mM Tris/HCl pH 7.5, 0.1 mM EGTA, 10 mM β-mercaptoethanol and 0.27 M sucrose.

Expression, Purification and Characterisation of the Kinase Domain of PDK1

A cDNA encoding for human PDK1 amino acid residues 51-359 with a stop codon inserted at position 360, was amplified by PCR reaction using full length human PDK1 cDNA in the pCMV5 vector [Alessi et al., 1997] as a template a 5′ primer, which incorporates a BamHI restriction site, an initiating methionine, a hexahistidine tag followed by a PreScission protease recognition sequence prior to the residue equivalent to Met51 of PDK1 (ggatcctataaatatggcacatcatcatcatcatcatctggaagttctgttccaggggcccatggacggcact gcagccgagcctcgg) (SEQ ID NO:106) and the 3′ primer applied in this reaction was: 5′-ggatcctcaggtgagcttcggaggcgtctgctggtg-3′ (SEQ ID NO: 107). The resulting PCR product was ligated into pCR 2.1 TOPO vector (Invitrogen) and then subcloned as a BamHI-BamHI fragment into pFastbac1 vector (Life Technologies) for baculovirus protein expression. The resulting construct was then used to generate recombinant baculovirus using the Bac-to-Bac system (Life Technologies) following the manufacturer's protocol. The resulting baculoviruses were used to infect Sf21 cells at 1.5×106/ml. The infected cells were harvested by centrifugation 72 hours post infection. Cell pellets corresponding to 7 l of culture were resuspended in 900 ml of Lysis Buffer and cells lysed in nitrogen cavitation chamber. Cell debris was then pelleted by centrifugation, the supernatant made 0.5 M NaCl by addition of 4M NaCl and then incubated with Ni-NTA-Agarose (10 ml resin) for one hour. The resin was then washed in 10 times with 40 ml of Lysis Buffer containing 0.5M NaCl and then placed in a disposable Econo-Pac column (BioRad), where the resin was further washed with 700 ml of high salt buffer and then with 100 ml of low salt buffer, both supplemented with 10 mM imidazole. Elution was performed with 200 mM imidazole in high salt buffer and 2 ml fractions were collected. Fractions containing protein were pooled, diluted to 200 mM NaCl with 25 mM Tris/HCl pH 7.5, and loaded onto a 5 ml Hi-trap Q sepharose column. The flow-through from this step, containing PDK1, was concentrated to 4 ml and then chromatographed on a 16/60 Superdex 200 gel filtration column using an AKTA Explorer system (Amersham Biosciences) equilibrated with high salt buffer with the addition of 1 mM DTT. PDK1 eluted in a large symmetric peak at the expected size for a monomer. The PDK1 containing peak was again pooled, concentrated and incubated with 300 μg GST-PreScission protease (expression construct kindly provided by John Heath, University of Birmingham, UK) on ice for 4 h. In order to eliminate the cleaved His-tag sequences as well as any remaining uncleaved His-PDK1 and the GST-PreScission protease, the mixture was incubated with a mixture of 200 μl glutathione-Sepharose and 200 μl Ni-NTA agarose resin for 15 minutes and the PDK1 protein that did not bind was collected. The resulting protein consists of PDK1 (51-359) preceded by a Gly-Pro at the N-terminus. The protein at this stage of the purification was apparently homogeneous as revealed by a single band after electrophoresis of 20 μg of protein on SDS-PAGE and staining with Coomasie Brilliant Blue 8250 (data not shown).

Electrospray mass spectrometry revealed a main peak mass close to the expected size of this fragment of PDK1. The specific activity of PDK1 (51-359) towards the peptide T308tide and its activation in the presence of PIFtide was identical to wild type full length PDK1 [Biondi et al., 2000], and tryptic peptide mass finger printing indicated that PDK1 was quantitatively phosphorylated at Ser241 (data not shown). In BiaCore experiments, the steady state binding of PDK1 (51-359) to the peptide PIFtide was similar to that of the His-tag PDK1 (51-556) protein characterised previously [Balendran et al., 1999a].

Crystallisation and Data Collection

The PDK1 (51-359) protein was concentrated to a final concentration of 8.5 mg/ml (as determined by a Bradford assay using bovine serum albumin as a standard). The sitting drop vapour diffusion method was used for producing crystals. Sitting drops were formed by mixing 1 μl of protein solution with 1 μl of a mother liquor solution (0.1 M Tris/HCl pH 8.5, 2.0 M ammonium sulphate, 16.6 mM ATP) with the addition of 0.2 μl EDTA (100 mM). Hexagonal crystals (Table I) of PDK1 were grown at 20° C. from a mother liquor containing 0.1M Tris/HCl pH 8.5, 2.0 M ammonium sulphate, 16.6 mM ATP). Crystals appeared after one day, growing to 0.05×0.05×0.2 mm over 20 days. Crystals were frozen in a nitrogen gas stream after being soaked in 0.075 M Tris 8.5, 1.5M ammonium sulphate, 25% (v/v) glycerol.

Expression and Purification of Wild Type and Mutant Forms of GST-PDK1.

Wild type-PDK1 [Alessi et al., 1997], PDK1[R76A], PDK1[R131A], PDK1[R76A,R131A], PDK1[T148A] and PDK1[Q150A] in the pEBG2T vector were used to express the wild type and indicated mutants of PDK1 fused through their N-terminus to glutathione S-transferase (GST). The GST fusion proteins were expressed in human embryonic kidney 293 cells. For the expression of each construct, twenty 10 cm diameter dishes of 293 cells were cultured and each dish transfected with 10 μg of the pEBG-2T construct, using a modified calcium phosphate method. 36 h post-transfection, the cells were lysed in 0.6 ml of ice-cold Buffer A, the lysates pooled, centrifuged at 4° C. for 10 min at 13000 g and the GST-fusion proteins were purified by affinity chromatography on glutathione-Sepharose and eluted in Buffer B supplemented with 20 mM glutathione as described previously [Alessi et al., 1997]. Typically between 1 and 2 mg of each GST-fusion protein was obtained and each protein was more than 75 judged by SDS polyacrylamide gel electrophoresis (data not shown).

PDK1 Catalytic Activity Measurements

The ability of wild type and mutant PDK1 to phosphorylate the synthetic peptide T308tide (KTFCGTPEYLAPEVRR ([Biondi et al., 2000]) (SEQ ID NO:108) was carried out in 30 μl assays containing 100 ng of wild type or mutant PDK1, 50 mM Tris/HCl pH 7.5, 0.1% 13-mercaptoethanol, 10 mM MgCl₂, 100 μM [32γ P]ATP (200 cpm/pmol), 0.5 μM microcystin-LR, 1 mM T308tide in the presence or absence of the indicated concentrations of the 56K-pHM peptide (SESANQVFLGFT(P)YVAPSV) (SEQ ID NO:104) or 56K-HM. peptide (SESANQVFLGFTYVAPSV) (SEQ ID NO:105). After incubation for 10 min at 30° C., 25 μl of the resultant mixture was spotted into P81 phosphocellulose paper (2×2 cm) and the papers washed and analysed as described previously for assays of MAP kinase. Control assays were carried out in parallel in which either PDK1, or peptide substrate were omitted; these values were always less than 5% of the activity measured in the presence of these reagents. One Unit of PDK1 activity was defined as that amount required to catalyse the phosphorylation of 1 nmol of the T308tide in 1 min.

Biacore Analysis

Binding was analysed in a BiaCore 3000 system (BiaCore AB, Stevenage, UK). Biotinylated S6K-pHM (Biotin-C₁₂-SESANQVFLGFT(P)YVAPSV) (SEQ ID NO:104) or the non-phosphorylated form of this peptide S6K-HM was bound to an streptavidin-coated Sensor chip (SA) (12 response units, RU). 30 μl of wild type or the indicated mutant GST-PDK1 were injected at a flow rate of 30 μl/min, in buffer HBS-P (10 mM HEPES pH 7.4, 0.15M NaCl, 0.005% (by vol) polysorbate-20) supplemented with 1 mM DTT. Specific interactions between 56K-pHM and PDK1 proteins were obtained between the concentration range of 2-2150 nM PDK1. Steady state binding was determined at each concentration. Dissociation of PDK1 from the phospho-peptide was monitored over a 1 min period. Regeneration of the sensor chip surface was performed with 1{tilde over (0)} μl injections of 0.05% SDS. As previously found for PDK1 binding to PIFtide [Biondi et al., 2000], the interaction data obtained using BiaCore did not fit to simple 1:1 interaction model. Apparent Kd values were estimated from the concentration of PDK1 which gives 50% of maximal response, which was obtained empirically using GST-PDK1[T148A] (RUmax=435). For all PDK1 construct tested, the off rates for S6Kp-HM were high in comparison to those of PIFtide binding with the time taken for 50% dissociation to occur for 56K-pHM is 30s compared to 1000s for PIFtide. This could account for the overall approximately 100-fold lower affinity of wild type PDK1 for 56K-pHM in comparison to PIFtide.

Data Collection, Structure Solution, and Refinement

Data on PDK1 crystals were collected at the European Synchrotron Radiation Facility (Grenoble, France) beamline ID14-EH1, using an ADSC Q4 CCD detector. The temperature of the crystals was maintained at 100K using a nitrogen cryostream. Data were processed using the HKL package [Otwinowski and Minor, 1997], statistics are shown in Table I.

The structure of PDK1 was solved by molecular replacement with AMoRe [Navaza, 1994] using the structure of PKA in complex with an inhibitory peptide as a search model (PDB entry 1YDB), against 8-4 Å data. A single, well separated solution was found with an R-factor of 0.479 (correlation coefficient=0.428). The structure was automatically built using warpNtrace [Perrakis et al., 1999], which found 262 of a possible 309 residues, giving an initial protein model with R=0.293 (Rfree=0.318) after simulated annealing in CNS [Brunger et al., 1998]. Iterative protein building in 0 [Jones et al., 1991] together with refinement in CNS, which included incorporation of a model for ATP, the phosphoserine in the activation loop, solvent molecules and a key sulphate molecule, resulted in a final model with R=0.195 (Rfree=0.222). No electron density was observed for residues 51-70 (the N-terminus of the construct) and 233-236 (the tip of the activation loop). All figures were made with PyMOL.

TABLE I Details of data collection & structure refinement for the PDK1 kinase domain. Values between brackets are for the highest resolution shell. All measured data were included in structure refinement. Wave length ( ) 0.933 Space group P3₂21 Unit cell ( ) a = 123.01, b = 123.01, c = 47.62 Resolution ( ) 25-2.0 (2.07-1.0) Observed reflections 77315 Unique reflections 27643 Redundancy 2.8 (2.5) Completeness (%) 98.0 (93.5) Rmerge 0.091 (0.454) I/sigma I 7.3 (2.0) R_(free) reflections 579 R_(cryst) 0.195 R_(free) 0.222 Number of groups °°Protein residues 71-359 °°Water 200 ATP 1 SO₄ 5 Glycerol 8 Wilson B (²) 22.4 <B> Protein 25.6 <B> Water 35.7 <B> ATP 38.8 RMSD from ideal geometry Bond lengths ( ) 0.005 Bond angles (°) 1.34 Main chain B (²) 1.5.

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Example 2 Co-Ordinates for PDK1Fragment with All Alternate Side Chains

REMARK coordinates from restrained individual B-factor refinement REMARK refinement resolution: 25.0 - 2.0 A REMARK starting r= 0.1972 free_r= 0.2220 REMARK final r= 0.1954 free_r= 0.2224 REMARK B rmsd for bonded mainchain atoms= 1.501 target= 1.5 REMARK B rmsd for bonded sidechain atoms= 2.235 target= 2.0 REMARK B rmsd for angle mainchain atoms= 2.347 target= 2.0 REMARK B rmsd for angle sidechain atoms= 3.302 target= 2.5 REMARK rweight= 0.0900 (with wa= 1.29263) REMARK target= mlf steps= 30 REMARK sg= P3(2)21 a= 123.013 b= 123.013 c= 47.624 alpha= 90 beta= 90 gamma= 120 REMARK parameter file 1 : /dd1/david/projects/PDK1_new/CNS/prot.par REMARK parameter file 2 : /dd1/david/projects/PDK1_new/CNS/atp.par REMARK parameter file 3 : CNS_TOPPAR:water_rep.param REMARK parameter file 4 : CNS_TOPPAR:ion.param REMARK parameter file 5 : /dd1/david/projects/PDK1_new/CNS/glycerol.par REMARK molecular structure file: . ./generate/alternate.mtf REMARK input coordinates: . . /minimize/minimize.pdb REMARK reflection file=. ./. . /1/hkl/cns.hkl REMARK ncs= none REMARK B-correction resolution: 6.0 - 2.0 REMARK initial B-factor correction applied to fobs : REMARK B11= −2.766 B22= −2.766 B33= 5.532 REMARK B12= −0.375 B13= 0.000 B23= 0.000 REMARK B-factor correction applied to coordinate array B: 0.031 0.031 REMARK bulk solvent: density level= 0.378441 e/A{circumflex over ( )}3, B-factor= 52.6885 A{circumflex over ( )}2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with |Fobs|> 10000 * rms(Fobs) rejected REMARK theoretical total number of refl. in resol. range: 28210 ( 100.0% ) REMARK number of unobserved reflections (no entry or |F|= 0): 568 ( 2.0% ) REMARK number of reflections rejected: 0 ( 0.0% ) REMARK total number of reflections used: 27642 ( 98.0% ) REMARK number of reflections in working set: 27063 ( 95.9% ) REMARK number of reflections in test set: 579 ( 2.1% ) CRYST1 123.013 123.013 47.624 90.00 90.00 120.00 P 32 2 1 REMARK FILENAME=“bindividual.pdb” REMARK DATE:Apr. 16, 2002 18:31:12 created by user: david REMARK VERSTON:1.0 ATOM 1 CB PRO A 71 58.912 −7.251 8.216 1.00 67.78 A ATOM 2 CC PRO A 71 59.621 −6.941 9.534 1.00 69.16 A ATOM 3 C PRO A 71 59.493 −6.506 5.894 1.00 67.06 A ATOM 4 O PRO A 71 59.196 −5.318 5.766 1.00 66.66 A ATOM 5 N PRO A 71 60.984 −6.073 7.833 1.00 67.86 A ATOM 6 CD PRO A 71 60.554 −5.762 9.207 1.00 68.24 A ATOM 7 CA PRO A 71 60.040 −7.03S 7.217 1.00 67.75 A ATOM 8 N PRO A 72 59.356 −7.38S 4.890 1.00 66.32 A ATOM 9 CD PRO A 72 59.712 −8.816 4.898 1.00 67.17 A ATOM 10 CA PRO A 72 58.840 −6.986 3.S78 1.00 65.61 A ATOM 11 CB PRO A 72 58.672 −8.321 2.8S8 1.00 66.47 A ATOM 12 CG PRO A 72 59.796 −9.133 3.419 1.00 67.57 A ATOM 13 C PRO A 72 57.527 −6.208 3.673 1.00 63.94 A ATOM 14 O PRO A 72 56.710 −6.451 4.561 1.00 64.11 A ATOM 15 N ALA A 73 57.341 −5.268 2.753 1.00 61.57 A ATOM 16 CA ALA A 73 56.133 −4.454 2.708 1.00 58.74 A ATOM 17 CB ALA A 73 56.438 −3.030 3.165 1.00 58.05 A ATOM 18 C ALA A 73 55.626 −4.448 1.271 1.00 56.78 A ATOM 19 O ALA A 73 56.347 −4.834 0.349 1.00 56.95 A ATOM 20 N PRO A 74 54.372 −4.024 1.057 1.00 54.15 A ATOM 21 CD PRO A 74 53.335 −3.610 2.018 1.00 53.31 A ATOM 22 CA PRO A 74 53.856 −4.003 −0.314 1.00 52.54 A ATOM 23 CB PRO A 74 52.474 −3.375 −0.148 1.00 52.86 A ATOM 24 CG PRO A 74 52.067 −3.824 1.226 1.00 52.88 A ATOM 25 C PRO A 74 54.772 −3.167 −1.204 1.00 50.08 A ATOM 26 O PRO A 74 55.559 −2.361 −0.708 1.00 49.96 A ATOM 27 N ALA A 75 54.680 −3.366 −2.514 1.00 47.58 A ATOM 28 CA ALA A 75 55.503 −2.602 −3.446 1.00 44.69 A ATOM 29 CB ALA A 75 55.312 −3.121 −4.870 1.00 46.14 A ATOM 30 C ALA A 75 55.100 −1.134 −3.371 1.00 41.55 A ATOM 31 O ALA A 75 53.947 −0.813 −3.086 1.00 41.01 A ATOM 32 N LYS A 76 56.053 −0.245 −3.619 1.00 38.31 A ATOM 33 CA LYS A 76 55.781 1.184 −3.588 1.00 35.72 A ATOM 34 CB LYS A 76 57.053 1.957 −3.930 1.00 37.70 A ATOM 35 CG LYS A 76 57.123 3.356 −3.350 1.00 40.99 A ATOM 36 CD LYS A 76 57.262 3.316 −1.836 1.00 40.04 A ATOM 37 CE LYS A 76 57.511 4.705 −1.277 1.00 42.08 A ATOM 38 NZ LYS A 76 57.681 4.695 0.202 1.00 42.99 A ATOM 39 C LYS A 76 54.708 1.467 −4.638 1.00 32.65 A ATOM 40 O LYS A 76 54.814 1.005 −5.770 1.00 31.41 A ATOM 41 N LYS A 77 53.668 2.207 −4.270 1.00 28.59 A ATOM 42 CA LYS A 77 52.619 2.517 −5.232 1.00 25.72 A ATOM 43 CB LYS A 77 51.316 2.865 −4.509 1.00 26.22 A ATOM 44 CG LYS A 77 50.796 1.731 −3.631 1.00 27.15 A ATOM 45 CD LYS A 77 49.487 2.089 −2.967 1.00 26.80 A ATOM 46 CE LYS A 77 49.136 1.091 −1.870 1.00 27.31 A ATOM 47 NZ LYS A 77 48.998 −0.296 −2.380 1.00 27.17 A ATOM 48 C LYS A 77 53.053 3.668 −6.137 1.00 24.67 A ATOM 49 O LYS A 77 54.010 4.377 −5.829 1.00 21.60 A ATOM 50 N ARG A 78 52.351 3.838 −7.254 1.00 23.66 A ATOM 51 CA ARG A 78 52.662 4.897 −8.211 1.00 26.14 A ATOM 52 CB ARG A 78 53.574 4.344 −9.318 1.00 28.57 A ATOM 53 CG ARG A 78 53.017 3.139 −10.050 1.00 34.78 A ATOM 54 CD ARG A 78 54.092 2.465 −10.896 1.00 40.96 A ATOM 55 NE ARG A 78 53.560 1.364 −11.700 1.00 48.93 A ATOM 56 CZ ARG A 78 52.985 0.270 −11.203 1.00 52.58 A ATOM 57 NH1 ARG A 78 52.860 0.113 −9.889 1.00 54.60 A ATOM 58 NH2 ARG A 78 52.530 −0.672 −12.022 1.00 54.09 A ATOM 59 C ARG A 78 51.382 5.488 −8.803 1.00 23.76 A ATOM 60 O ARG A 78 50.311 4.888 −8.706 1.00 24.25 A ATOM 61 N PRO A 79 51.475 6.676 −9.428 1.00 21.76 A ATOM 62 CD PRO A 79 52.691 7.475 −9.668 1.00 20.82 A ATOM 63 CA PRO A 79 50.301 7.325 −10.021 1.00 21.96 A ATOM 64 CB PRO A 79 50.910 8.481 −10.816 1.00 22.27 A ATOM 65 CG PRO A 79 52.124 8.831 −10.014 1.00 22.12 A ATOM 66 C PRO A 79 49.446 6.413 −10.903 1.00 22.86 A ATOM 67 O PRO A 79 48.213 6.461 −10.842 1.00 20.52 A ATOM 68 N GLU A 80 50.103 5.586 −11.714 1.00 21.87 A ATOM 69 CA GLU A 80 49.403 4.685 −12.628 1.00 22.99 A ATOM 70 CB GLU 80 50.393 3.994 −13.571 0.50 25.24 AC1 ATOM 71 CG GLU 80 51.230 2.907 −12.925 0.50 28.75 AC1 ATOM 72 CD GLU 80 52.157 2.224 −13.913 0.50 31.99 AC1 ATOM 73 OE1 GLU 80 53.072 2.897 −14.433 0.50 34.34 AC1 ATOM 74 OE2 GLU 80 51.969 1.015 −14.172 0.50 32.83 AC1 ATOM 75 C GLU A 80 48.556 3.631 −11.912 1.00 22.09 A ATOM 76 O GLU A 80 47.692 3.013 −12.530 1.00 22.37 A ATOM 77 N ASP A 81 48.804 3.413 −10.622 1.00 19.97 A ATOM 78 CA ASP A 81 48.026 2.423 −9.874 1.00 19.93 A ATOM 79 CB ASP A 81 48.736 2.029 −8.571 1.00 21.19 A ATOM 80 CG ASP A 81 50.089 1.380 −8.807 1.00 22.46 A ATOM 81 OD1 ASP A 81 50.195 0.554 −9.731 1.00 24.22 A ATOM 82 OD2 ASP A 81 51.043 1.685 −8.058 1.00 23.33 A ATOM 83 C ASP A 81 46.652 2.975 −9.518 1.00 20.85 A ATOM 84 O ASP A 81 45.793 2.246 −9.015 1.00 19.96 A ATOM 85 N PHE A 82 46.445 4.258 −9.804 1.00 18.91 A ATOM 86 CA PHE A 82 45.200 4.934 −9.465 1.00 19.30 A ATOM 87 CB PHE A 82 45.475 6.027 −8.427 1.00 18.43 A ATOM 88 CG PHE A 82 46.134 5.531 −7.175 1.00 18.01 A ATOM 89 CD1 PHE A 82 45.371 5.136 −6.084 1.00 17.19 A ATOM 90 CD2 PHE A 82 47.520 5.460 −7.086 1.00 18.99 A ATOM 91 CE1 PHE A 82 45.977 4.676 −4.918 1.00 17.12 A ATOM 92 CE2 PHE A 82 48.137 5.000 −5.925 1.00 19.64 A ATOM 93 CZ PHE A 82 47.361 4.607 −4.838 1.00 18.00 A ATOM 94 C PHE A 82 44.476 5.596 −10.621 1.00 20.81 A ATOM 95 O PHE A 82 45.066 5.933 −11.649 1.00 20.34 A ATOM 96 N LYS A 83 43.182 5.792 −10.411 1.00 19.80 A ATOM 97 CA LYS A 83 42.321 6.478 −11.353 1.00 21.65 A ATOM 98 CB LYS A 83 41.096 5.625 −11.687 1.00 22.02 A ATOM 99 CG LYS A 83 40.062 6.326 −12.550 1.00 28.93 A ATOM 100 CD LYS A 83 38.974 5.355 −12.981 1.00 34.20 A ATOM 101 CE LYS A 83 37.909 6.042 −13.824 1.00 38.10 A ATOM 102 NZ LYS A 83 37.179 7.086 −13.043 1.00 43.33 A ATOM 103 C LYS A 83 41.913 7.702 −10.541 1.00 20.74 A ATOM 104 O LYS A 83 41.084 7.606 −9.635 1.00 20.98 A ATOM 105 N PHE A 84 42.513 8.848 −10.835 1.00 19.99 A ATOM 106 CA PHE A 84 42.188 10.049 −10.083 1.00 18.63 A ATOM 107 CB PHE A 84 43.279 11.103 −10.258 1.00 18.95 A ATOM 108 CG PHE A 84 44.571 10.741 −9.587 1.00 17.68 A ATOM 109 CD1 PHE A 84 45.498 9.926 −10.224 1.00 18.16 A ATOM 110 CD2 PHE A 84 44.843 11.183 −8.299 1.00 19.66 A ATOM 111 CE1 PHE A 84 46.676 9.556 −9.589 1.00 18.09 A ATOM 112 CE2 PHE A 84 46.021 10.816 −7.653 1.00 18.89 A ATOM 113 CZ PHE A 84 46.936 10.002 −8.301 1.00 17.33 A ATOM 114 C PHE A 84 40.834 10.617 −10.460 1.00 19.69 A ATOM 115 O PHE A 84 40.391 10.489 −11.601 1.00 20.72 A ATOM 116 N GLY A 85 40.178 11.233 −9.484 1.00 16.80 A ATOM 117 CA GLY A 85 38.872 11.810 −9.716 1.00 17.73 A ATOM 118 C GLY A 85 38.819 13.280 −9.346 1.00 18.75 A ATOM 119 O GLY A 85 39.740 14.043 −9.650 1.00 18.45 A ATOM 120 N LYS A 86 37.753 13.673 −8.659 1.00 16.00 A ATOM 121 CA LYS A 86 37.571 15.064 −8.278 1.00 18.26 A ATOM 122 CB LYS A 86 36.133 15.302 −7.812 1.00 19.00 A ATOM 123 CG LYS A 86 35.793 14.660 −6.481 1.00 21.55 A ATOM 124 CD LYS A 86 34.368 14.981 −6.066 1.00 26.48 A ATOM 125 CE LYS A 86 33.994 14.239 −4.793 1.00 31.92 A ATOM 126 NZ LYS A 86 32.568 14.457 −4.412 1.00 35.36 A ATOM 127 C LYS A 86 38.523 15.571 −7.202 1.00 18.57 A ATOM 128 O LYS A 86 39.045 14.807 −6.385 1.00 16.77 A ATOM 129 N ILE A 87 38.737 16.881 −7.227 1.00 17.88 A ATOM 130 CA ILE A 87 39.577 17.554 −6.256 1.00 18.26 A ATOM 131 CB ILE A 87 39.994 18.952 −6.772 1.00 19.60 A ATOM 132 CG2 ILE A 87 40.593 19.786 −5.628 1.00 18.73 A ATOM 133 CG1 ILE A 87 40.968 18.786 −7.945 1.00 21.16 A ATOM 134 CD1 ILE A 87 41.412 20.087 −8.588 1.00 25.26 A ATOM 135 C ILE A 87 38.731 17.709 −4.997 1.00 19.67 A ATOM 136 O ILE A 87 37.628 18.249 −5.052 1.00 20.41 A ATOM 137 N LEU A 88 39.240 17.229 −3.867 1.00 19.15 A ATOM 138 CA LEU A 88 38.508 17.324 −2.611 1.00 20.68 A ATOM 139 CB LEU A 88 38.870 16.151 −1.700 1.00 19.97 A ATOM 140 CG LEU A 88 38.529 14.759 −2.237 1.00 19.24 A ATOM 141 CD1 LEU A 88 39.090 13.692 −1.311 1.00 21.41 A ATOM 142 CD2 LEU A 88 37.029 14.622 −2.359 1.00 18.84 A ATOM 143 C LEU A 88 38.815 18.632 −1.901 1.00 23.11 A ATOM 144 O LEU A 88 37.999 19.146 −1.139 1.00 25.10 A ATOM 145 N GLY A 89 39.997 19.174 −2.149 1.00 24.09 A ATOM 146 CA GLY A 89 40.367 20.418 −1.507 1.00 24.27 A ATOM 147 C GLY A 89 41.658 20.954 −2.078 1.00 25.47 A ATOM 148 O GLY A 89 42.445 20.202 −2.666 1.00 22.19 A ATOM 149 N GLU A 90 41.870 22.254 −1.906 1.00 26.22 A ATOM 150 CA GLU A 90 43.064 22.924 −2.404 1.00 29.96 A ATOM 151 CB GLU A 90 42.698 23.814 −3.596 1.00 30.75 A ATOM 152 CG GLU A 90 42.267 23.038 −4.831 1.00 34.32 A ATOM 153 CD GLU A 90 41.711 23.930 −5.927 1.00 38.27 A ATOM 154 OE1 GLU A 90 40.590 24.456 −5.764 1.00 40.57 A ATOM 155 0E2 GLU A 90 42.398 24.110 −6.952 1.00 40.90 A ATOM 156 C GLU A 90 43.711 23.768 −1.313 1.00 30.68 A ATOM 157 O GLU A 90 43.049 24.574 −0.668 1.00 32.83 A ATOM 158 N GLY A 91 45.006 23.566 −1.104 1.00 29.66 A ATOM 159 CA GLY A 91 45.724 24.332 −0.104 1.00 29.40 A ATOM 160 C GLY A 91 46.795 25.151 −0.798 1.00 29.98 A ATOM 161 O GLY A 91 46.894 25.130 −2.028 1.00 28.16 A ATOM 162 N SER A 92 47.605 25.870 −0.029 1.00 28.30 A ATOM 163 CA SER A 92 48.653 26.681 −0.633 1.00 30.50 A ATOM 164 CB SER A 92 49.165 27.717 −0.370 1.00 32.43 A ATOM 165 OG SER A 92 49.520 27.099 −1.593 1.00 40.94 A ATOM 166 C SER A 92 49.815 25.843 −1.164 1.00 29.77 A ATOM 167 O SER A 92 50.456 26.221 −2.143 1.00 30.46 A ATOM 168 N PHE A 93 50.087 24.703 −0.536 1.00 27.65 A ATOM 169 CA PHE A 93 51.185 23.855 −0.995 1.00 26.34 A ATOM 170 CB PHE A 93 52.281 23.785 −0.068 1.00 27.95 A ATOM 171 CG PHE A 93 52.861 25.117 −0.406 1.00 31.06 A ATOM 172 CD1 PHE A 93 52.283 25.909 −1.392 1.00 29.96 A ATOM 173 CD2 PHE A 93 53.949 25.613 −0.308 1.00 31.38 A ATOM 174 CE1 PHE A 93 52.779 27.181 −1.665 1.00 32.69 A ATOM 175 CE2 PHE A 93 54.452 26.883 −0.044 1.00 32.63 A ATOM 176 CZ PHE A 93 53.864 27.670 −0.945 1.00 31.81 A ATOM 177 C PHE A 93 50.759 22.445 −1.365 1.00 25.39 A ATOM 178 O PHE A 93 51.601 21.559 −1.522 1.00 24.59 A ATOM 179 N SER A 94 49.457 22.235 −1.519 1.00 23.63 A ATOM 180 CA SER A 94 48.965 20.912 −1.860 1.00 21.43 A ATOM 181 CB SER A 94 49.017 20.013 −0.628 1.00 21.42 A ATOM 182 OG SER A 94 48.091 20.475 −0.340 1.00 21.19 A ATOM 183 C SER A 94 47.539 20.925 −2.378 1.00 19.82 A ATOM 184 O SER A 94 46.795 21.882 −2.173 1.00 18.76 A ATOM 185 N THR A 95 47.174 19.832 −3.038 1.00 19.38 A ATOM 186 CA THR A 95 45.840 19.637 −3.580 1.00 17.98 A ATOM 187 CB THR A 95 45.818 19.818 −5.110 1.00 19.25 A ATOM 188 OG1 THR A 95 46.196 21.162 −5.434 1.00 22.04 A ATOM 189 CG2 THR A 95 44.421 19.549 −5.661 1.00 17.61 A ATOM 190 C THR A 95 45.455 18.201 −3.243 1.00 18.61 A ATOM 191 O THR A 95 46.212 17.264 −3.524 1.00 17.10 A ATOM 192 N VAL A 96 44.295 18.024 −2.623 1.00 16.53 A ATOM 193 CA VAL A 96 43.845 16.685 −2.266 1.00 16.05 A ATOM 194 CB VAL A 96 43.170 16.672 −0.886 1.00 16.32 A ATOM 195 CG1 VAL A 96 42.741 15.249 −0.532 1.00 18.02 A ATOM 196 CG2 VAL A 96 44.145 17.206 −0.168 1.00 16.69 A ATOM 197 C VAL A 96 42.875 16.207 −3.335 1.00 16.42 A ATOM 198 O VAL A 96 41.906 16.892 −3.665 1.00 16.47 A ATOM 199 N VAL A 97 43.157 15.033 −3.888 1.00 16.80 A ATOM 200 CA VAL A 97 42.338 14.471 −4.949 1.00 16.72 A ATOM 201 CB VAL A 97 43.153 14.354 −6.255 1.00 18.43 A ATOM 202 CG1 VAL A 97 42.249 13.927 −7.404 1.00 19.69 A ATOM 203 CG2 VAL A 97 43.831 15.685 −6.569 1.00 17.84 A ATOM 204 C VAL A 97 41.812 13.091 −4.583 1.00 16.77 A ATOM 205 O VAL A 97 42.532 12.270 −4.014 1.00 17.13 A ATOM 206 N LEU A 98 40.545 12.845 −4.895 1.00 16.62 A ATOM 207 CA LEU A 98 39.947 11.548 −4.624 1.00 17.04 A ATOM 208 CB LEU A 98 38.424 11.633 −4.743 1.00 16.89 A ATOM 209 CG LEU A 98 37.635 10.342 −4.508 1.00 19.46 A ATOM 210 CD1 LEU A 98 37.990 9.762 −3.146 1.00 20.07 A ATOM 211 CD2 LEU A 98 36.143 10.627 −4.588 1.00 17.93 A ATOM 212 C LEU A 98 40.512 10.597 −5.677 1.00 17.38 A ATOM 213 O LEU A 98 40.527 10.920 −6.863 1.00 18.60 A ATOM 214 N ALA A 99 40.995 9.438 −5.246 1.00 17.13 A ATOM 215 CA ALA A 99 41.570 8.466 −6.168 1.00 18.42 A ATOM 216 CB ALA A 99 43.090 8.524 −6.105 1.00 14.76 A ATOM 217 C ALA A 99 41.102 7.055 −5.848 1.00 21.40 A ATOM 218 O ALA A 99 40.941 6.691 −4.679 1.00 22.52 A ATOM 219 N ARG A 100 40.878 6.261 −6.888 1.00 19.77 A ATOM 220 CA ARG A 100 40.459 4.884 −6.693 1.00 20.85 A ATOM 221 CB ARG A 100 39.202 4.585 −7.518 1.00 24.22 A ATOM 222 CG ARG A 100 38.608 3.205 −7.256 1.00 31.78 A ATOM 223 CD ARG A 100 37.326 2.979 −8.048 1.00 36.24 A ATOM 224 NE ARG A 100 36.213 3.818 −7.594 1.00 41.40 A ATOM 225 CZ ARG A 100 35.566 3.662 −6.439 1.00 42.05 A ATOM 226 NH1 ARG A 100 35.912 2.696 −5.598 1.00 40.67 A ATOM 227 NH2 ARG A 100 34.559 4.468 −6.128 1.00 43.65 A ATOM 228 C ARG A 100 41.613 3.985 −7.129 1.00 18.63 A ATOM 229 O ARG A 100 42.078 4.065 −8.271 1.00 19.49 A ATOM 230 N GLU A 101 42.102 3.157 −6.212 1.00 16.43 A ATOM 231 CA GLU A 101 43.196 2.246 −6.533 1.00 16.11 A ATOM 232 CB GLU A 101 43.774 1.637 −5.248 1.00 16.79 A ATOM 233 CG GLU A 101 44.917 0.657 −5.488 1.00 16.51 A ATOM 234 CD GLU A 101 45.501 0.115 −4.200 1.00 18.20 A ATOM 235 OE1 GLU A 101 44.733 −0.081 −3.239 1.00 18.32 A ATOM 236 OE2 GLU A 101 46.725 −0.132 −4.150 1.00 17.14 A ATOM 237 C GLU A 101 42.625 1.152 −7.442 1.00 17.92 A ATOM 238 O GLU A 101 41.681 0.462 −7.069 1.00 18.02 A ATOM 239 N LEU A 102 43.198 1.002 −8.632 1.00 19.06 A ATOM 240 CA LEU A 102 42.718 0.025 −9.607 1.00 20.71 A ATOM 241 CB LEU A 102 43.569 0.097 −10.878 1.00 23.42 A ATOM 242 CG LEU A 102 43.531 1.426 −11.642 1.00 25.30 A ATOM 243 CD1 LEU A 102 44.577 1.414 −12.748 1.00 27.88 A ATOM 244 CD2 LEU A 102 42.140 1.647 −12.214 1.00 26.79 A ATOM 245 C LEU A 102 42.671 −1.418 −9.125 1.00 21.62 A ATOM 246 O LEU A 102 41.668 −2.103 −9.305 1.00 21.09 A ATOM 247 N ALA A 103 43.753 −1.874 −8.507 1.00 19.38 A ATOM 248 CA ALA A 103 43.836 −3.249 −8.035 1.00 20.87 A ATOM 249 CB ALA A 103 45.284 −3.571 −7.671 1.00 19.23 A ATOM 250 C ALA A 103 42.919 −3.629 −6.872 1.00 19.92 A ATOM 251 O ALA A 103 42.703 −4.815 −6.628 1.00 20.38 A ATOM 252 N THR A 104 42.361 −2.643 −6.175 1.00 18.12 A ATOM 253 CA THR A 104 41.517 −2.927 −5.018 1.00 17.15 A ATOM 254 CB THR A 104 42.212 −2.484 −3.717 1.00 19.54 A ATOM 255 CC1 THR A 104 42.456 −1.070 −3.773 1.00 19.26 A ATOM 256 CC2 THR A 104 43.536 −3.219 −3.529 1.00 17.02 A ATOM 257 C THR A 104 40.159 −2.247 −5.026 1.00 19.44 A ATOM 258 O THR A 104 39.259 −2.648 −4.285 1.00 18.70 A ATOM 259 N SER A 105 40.034 −1.207 −5.847 1.00 19.65 A ATOM 260 CA SER A 105 38.819 −0.400 −5.967 1.00 19.37 A ATOM 261 CB SER 105 37.598 −1.304 −6.173 0.50 21.81 AC1 ATOM 262 OG SER 105 36.431 −0.539 −6.412 0.50 23.01 AC1 ATOM 263 C SER A 105 38.644 0.447 −4.701 1.00 18.99 A ATOM 264 O SER A 105 37.602 1.070 −4.488 1.00 18.66 A ATOM 265 N ARC A 106 39.674 0.468 −3.861 1.00 16.84 A ATOM 266 CA ARC A 106 39.655 1.267 −2.634 1.00 16.21 A ATOM 267 CB ARC A 106 40.827 0.886 −1.723 1.00 16.41 A ATOM 268 CC ARC A 106 40.619 −0.367 −0.906 1.00 15.49 A ATOM 269 CD ARC A 106 41.887 −0.755 −0.170 1.00 17.43 A ATOM 270 NE ARC A 106 41.620 −1.792 0.824 1.00 20.47 A ATOM 271 CZ ARC A 106 42.548 −2.568 1.371 1.00 20.24 A ATOM 272 NH1 ARC A 106 43.821 −2.433 1.017 1.00 17.80 A ATOM 273 NH2 ARC A 106 42.198 −3.468 2.285 1.00 20.14 A ATOM 274 C ARC A 106 39.785 2.746 −2.981 1.00 17.37 A ATOM 275 O ARC A 106 40.514 3.103 −3.902 1.00 17.75 A ATOM 276 N CLU A 107 39.085 3.599 −2.240 1.00 16.06 A ATOM 277 CA CLU A 107 39.156 5.039 −2.461 1.00 20.80 A ATOM 278 CB CLU A 107 37.779 5.694 −2.337 1.00 22.93 A ATOM 279 CC CLU A 107 36.711 5.171 −3.269 1.00 30.87 A ATOM 280 CD CLU A 107 35.431 5.975 −3.148 1.00 32.40 A ATOM 281 OE1 CLU A 107 35.262 6.939 −3.923 1.00 33.74 A ATOM 282 OE2 CLU A 107 34.608 5.654 −2.263 1.00 36.00 A ATOM 283 C CLU A 107 40.053 5.678 −1.410 1.00 18.93 A ATOM 284 O CLU A 107 39.891 5.427 −0.220 1.00 19.21 A ATOM 285 N TYR A 108 40.988 6.507 −1.852 1.00 16.70 A ATOM 286 CA TYR A 108 41.883 7.209 −0.942 1.00 15.86 A ATOM 287 CB TYR A 108 43.325 6.728 −1.104 1.00 15.30 A ATOM 288 CC TYR A 108 43.593 5.328 −0.612 1.00 16.33 A ATOM 289 CD1 TYR A 108 43.765 5.066 0.746 1.00 16.36 A ATOM 290 CE1 TYR A 108 44.046 3.769 1.201 1.00 18.48 A ATOM 291 CD2 TYR A 108 43.701 4.268 −1.511 1.00 13.25 A ATOM 292 CE2 TYR A 108 43.980 2.981 −1.075 1.00 17.28 A ATOM 293 CZ TYR A 108 44.152 2.736 0.276 1.00 19.17 A ATOM 294 OH TYR A 108 44.440 1.461 0.688 1.00 19.38 A ATOM 295 C TYR A 108 41.850 8.687 −1.292 1.00 16.80 A ATOM 296 O TYR A 108 41.560 9.058 −2.431 1.00 15.22 A ATOM 297 N ALA A 109 42.132 9.528 −0.306 1.00 14.61 A ATOM 298 CA ALA A 109 42.207 10.957 −0.539 1.00 14.30 A ATOM 299 CB ALA A 109 41.671 11.726 0.661 1.00 14.78 A ATOM 300 C ALA A 109 43.713 11.136 −0.667 1.00 16.79 A ATOM 301 O ALA A 109 44.450 10.983 0.317 1.00 16.52 A ATOM 302 N ILE A 110 44.182 11.410 −1.881 1.00 14.80 A ATOM 303 CA ILE A 110 45.609 11.574 −2.093 1.00 15.80 A ATOM 304 CB ILE A 110 46.065 10.863 −3.396 1.00 16.85 A ATOM 305 CC2 ILE A 110 47.550 11.098 −3.632 1.00 16.80 A ATOM 306 CC1 ILE A 110 45.774 9.358 −3.284 1.00 17.76 A ATOM 307 CD1 ILE A 110 46.308 8.513 −4.437 1.00 16.07 A ATOM 308 C ILE A 110 46.004 13.045 −2.129 1.00 17.78 A ATOM 309 O ILE A 110 45.534 13.813 −2.976 1.00 16.24 A ATOM 310 N LYS A 111 46.846 13.435 −1.177 1.00 16.15 A ATOM 311 CA LYS A 111 47.326 14.808 −1.100 1.00 17.20 A ATOM 312 CB LYS A 111 47.700 15.176 0.344 1.00 17.41 A ATOM 313 CG LYS A 111 48.350 16.547 0.464 1.00 20.71 A ATOM 314 CD LYS A 111 48.585 16.971 1.910 1.00 24.25 A ATOM 315 CE LYS A 111 47.288 17.381 2.598 1.00 29.46 A ATOM 316 NZ LYS A 111 47.516 17.866 4.000 1.00 30.50 A ATOM 317 C LYS A 111 48.551 14.890 −1.994 1.00 16.41 A ATOM 318 O LYS A 111 49.509 14.137 −1.813 1.00 18.20 A ATOM 319 N ILE A 112 48.509 15.798 −2.963 1.00 15.87 A ATOM 320 CA ILE A 112 49.606 15.967 −3.907 1.00 17.28 A ATOM 321 CB ILE A 112 49.079 15.911 −5.358 1.00 16.43 A ATOM 322 CG2 ILE A 112 50.235 15.998 −6.341 1.00 15.12 A ATOM 323 CG1 ILE A 112 48.293 14.609 −5.565 1.00 16.82 A ATOM 324 CD1 ILE A 112 47.580 14.511 −6.904 1.00 18.47 A ATOM 325 C ILE A 112 50.307 17.301 −3.663 1.00 19.03 A ATOM 326 O ILE A 112 49.669 18.350 −3.635 1.00 19.15 A ATOM 327 N LEU A 113 51.622 17.245 −3.472 1.00 20.22 A ATOM 328 CA LEU A 113 52.416 18.442 −3.214 1.00 22.36 A ATOM 329 CB LEU A 113 52.995 18.397 −1.794 1.00 22.13 A ATOM 330 CG LEU A 113 52.042 18.063 −0.646 1.00 22.46 A ATOM 331 CD1 LEU A 113 51.866 16.557 −0.553 1.00 23.81 A ATOM 332 CD2 LEU A 113 52.603 18.595 0.660 1.00 23.68 A ATOM 333 C LEU A 113 53.560 18.547 −4.215 1.00 23.37 A ATOM 334 O LEU A 113 54.300 17.586 −4.424 1.00 23.11 A ATOM 335 N GLU A 114 53.706 19.714 −4.834 1.00 23.88 A ATOM 336 CA GLU A 114 54.771 19.920 −5.806 1.00 26.00 A ATOM 337 CB GLU A 114 54.435 21.111 −6.706 1.00 27.74 A ATOM 338 CG GLU A 114 55.533 21.452 −7.696 1.00 35.07 A ATOM 339 CD GLU A 114 55.220 22.696 −8.497 1.00 39.24 A ATOM 340 OE1 GLU A 114 54.808 23.703 −7.885 1.00 41.45 A ATOM 341 OE2 GLU A 114 55.395 22.670 −9.736 1.00 44.05 A ATOM 342 C GLU A 114 56.087 20.163 −5.067 1.00 24.37 A ATOM 343 O GLU A 114 56.186 21.071 −4.238 1.00 24.43 A ATOM 344 N LYS A 115 57.096 19.350 −5.360 1.00 24.10 A ATOM 345 CA LYS A 115 58.376 19.493 −4.678 1.00 24.93 A ATOM 346 CB LYS A 115 59.339 18.373 −5.103 1.00 23.72 A ATOM 347 CG LYS A 115 59.139 17.080 −4.308 1.00 23.09 A ATOM 348 CD LYS A 115 60.064 15.944 −4.743 1.00 21.92 A ATOM 349 CE LYS A 115 59.691 15.400 −6.117 1.00 22.42 A ATOM 350 NZ LYS A 115 60.447 14.150 −6.448 1.00 19.71 A ATOM 351 C LYS A 115 59.031 20.858 −4.868 1.00 26.87 A ATOM 352 O LYS A 115 59.492 21.469 −3.903 1.00 26.17 A ATOM 353 N ARG A 116 59.058 21.348 −6.102 1.00 28.73 A ATOM 354 CA ARG A 116 59.678 22.638 −6.380 1.00 29.66 A ATOM 355 CB ARG 116 59.533 22.980 −7.868 0.50 31.29 AC1 ATOM 356 CG ARG 116 60.047 24.361 −8.267 0.50 33.19 AC1 ATOM 357 CD ARG 116 61.368 24.710 −7.590 0.50 35.13 AC1 ATOM 358 NE ARG 116 62.329 23.612 −7.618 0.50 36.42 AC1 ATOM 359 CZ ARG 116 63.510 23.648 −7.009 0.50 36.18 AC1 ATOM 360 NH1 ARG 116 63.871 24.729 −6.332 0.50 36.12 AC1 ATOM 361 NH2 ARG 116 64.324 22.602 −7.067 0.50 35.77 AC1 ATOM 362 C ARG A 116 59.097 23.761 −5.519 1.00 29.70 A ATOM 363 O ARG A 116 59.843 24.515 −4.889 1.00 29.16 A ATOM 364 N HIS A 117 57.773 23.862 −5.472 1.00 27.22 A ATOM 365 CA HIS A 117 57.126 24.903 −4.681 1.00 26.33 A ATOM 366 CB HIS A 117 55.606 24.835 −4.848 1.00 28.41 A ATOM 367 CG HIS A 117 54.881 26.00 −54.258 1.00 31.82 A ATOM 368 CD2 HIS A 117 55.309 27.24 −93.935 1.00 33.19 A ATOM 369 ND1 HIS A 117 53.536 25.97 −43.961 1.00 34.30 A ATOM 370 CE1 HIS A 117 53.165 27.14 −83.480 1.00 34.58 A ATOM 371 NE2 HIS A 117 54.222 27.94 −03.455 1.00 35.18 A ATOM 372 C HIS A 117 57.477 24.78 −03.202 1.00 26.22 A ATOM 373 O HIS A 117 57.737 25.77 −62.534 1.00 25.67 A ATOM 374 N ILE A 118 57.469 23.554 −2.689 1.00 24.94 A ATOM 375 CA ILE A 118 57.792 23.315 −1.285 1.00 23.94 A ATOM 376 CB ILE A 118 57.711 21.812 −0.952 1.00 23.50 A ATOM 377 CG2 ILE A 118 58.374 21.533 0.389 1.00 23.76 A ATOM 378 CG1 ILE A 118 56.246 21.362 −0.959 1.00 24.42 A ATOM 379 CD1 ILE A 118 56.066 19.858 −0.834 1.00 28.06 A ATOM 380 C ILE A 118 59.195 23.821 −0.958 1.00 23.78 A ATOM 381 O ILE A 118 59.402 24.495 −0.048 1.00 23.49 A ATOM 382 N ILE A 119 60.153 23.489 −1.815 1.00 23.46 A ATOM 383 CA ILE A 119 61.534 23.913 −1.619 1.00 25.13 A ATOM 384 CB ILE A 119 62.467 23.250 −2.664 1.00 24.25 A ATOM 385 CG2 ILE A 119 63.858 23.890 −2.617 1.00 22.47 A ATOM 386 CG1 ILE A 119 62.540 21.738 −2.395 1.00 25.05 A ATOM 387 CD1 ILE A 119 63.327 20.945 −3.439 1.00 24.62 A ATOM 388 C ILE A 119 61.667 25.435 −1.705 1.00 25.96 A ATOM 389 O ILE A 119 62.330 26.051 −0.872 1.00 24.78 A ATOM 390 N LYS A 120 61.028 26.039 −2.704 1.00 27.67 A ATOM 391 CA LYS A 120 61.100 27.489 −2.879 1.00 30.29 A ATOM 392 CB LYS A 120 60.242 27.940 −4.060 1.00 32.34 A ATOM 393 CG LYS A 120 60.674 27.407 −5.409 1.00 39.30 A ATOM 394 CD LYS A 120 59.765 27.950 −6.512 1.00 45.19 A ATOM 395 CE LYS A 120 58.294 27.636 −6.218 1.00 46.48 A ATOM 396 NZ LYS A 120 57.363 28.155 −7.252 1.00 46.49 A ATOM 397 C LYS A 120 60.647 28.247 −1.638 1.00 30.89 A ATOM 398 O LYS A 120 61.303 29.198 −1.217 1.00 32.48 A ATOM 399 N GLU A 121 59.527 27.825 −1.055 1.00 29.82 A ATOM 400 CA GLU A 121 58.986 28.488 0.128 1.00 30.33 A ATOM 401 CB GLU A 121 57.455 28.416 0.117 1.00 33.04 A ATOM 402 CG GLU A 121 56.794 29.021 −1.120 1.00 36.45 A ATOM 403 CD GLU A 121 57.221 30.456 −1.373 1.00 39.88 A ATOM 404 OE1 GLU A 121 57.200 31.264 −0.420 1.00 40.53 A ATOM 405 OE2 GLU A 121 57.573 30.778 −2.529 1.00 43.24 A ATOM 406 C GLU A 121 59.511 27.930 1.451 1.00 30.37 A ATOM 407 O GLU A 121 58.946 28.204 2.513 1.00 31.24 A ATOM 408 N ASN A 122 60.588 27.151 1.390 1.00 29.03 A ATOM 409 CA ASN A 122 61.183 26.573 2.594 1.00 28.46 A ATOM 410 CB ASN A 122 61.836 27.673 3.436 1.00 31.28 A ATOM 411 CG ASN A 122 62.945 28.395 2.698 1.00 34.12 A ATOM 412 OD1 ASN A 122 62.697 29.143 1.754 1.00 35.57 A ATOM 413 ND2 ASN A 122 64.181 28.169 3.127 1.00 35.73 A ATOM 414 C ASN A 122 60.157 25.835 3.456 1.00 26.89 A ATOM 415 O ASN A 122 60.085 26.055 4.663 1.00 27.23 A ATOM 416 N LYS A 123 59.375 24.955 2.842 1.00 23.99 A ATOM 417 CA LYS A 123 58.358 24.210 3.574 1.00 22.43 A ATOM 418 CB LYS A 123 57.031 24.248 2.810 1.00 21.97 A ATOM 419 CG LYS A 123 56.475 25.645 2.599 1.00 25.68 A ATOM 420 CD LYS A 123 56.253 26.354 3.927 1.00 27.54 A ATOM 421 CE LYS A 123 55.822 27.796 3.716 1.00 31.30 A ATOM 422 NZ LYS A 123 55.756 28.540 5.004 1.00 33.21 A ATOM 423 C LYS A 123 58.748 22.759 3.821 1.00 22.20 A ATOM 424 O LYS A 123 57.924 21.960 4.264 1.00 22.50 A ATOM 425 N VAL A 124 59.997 22.412 3.535 1.00 20.59 A ATOM 426 CA VAL A 124 60.439 21.039 3.730 1.00 20.25 A ATOM 427 CB VAL A 124 61.922 20.850 3.328 1.00 19.43 A ATOM 428 CG1 VAL A 124 62.346 19.407 3.573 1.00 18.69 A ATOM 429 CG2 VAL A 124 62.104 21.195 1.853 1.00 18.21 A ATOM 430 C VAL A 124 60.236 20.561 5.163 1.00 19.53 A ATOM 431 O VAL A 124 59.841 19.418 5.385 1.00 20.02 A ATOM 432 N PRO A 125 60.513 21.422 6.159 1.00 20.01 A ATOM 433 CD PRO A 125 61.178 22.738 6.118 1.00 18.69 A ATOM 434 CA PRO A 125 60.318 20.979 7.544 1.00 19.88 A ATOM 435 CB PRO A 125 60.793 22.180 8.363 1.00 19.95 A ATOM 436 CG PRO A 125 61.839 22.805 7.479 1.00 18.85 A ATOM 437 C PRO A 125 58.848 20.642 7.824 1.00 19.76 A ATOM 438 O PRO A 125 58.544 19.700 8.550 1.00 16.99 A ATOM 439 N TYR A 126 57.947 21.418 7.235 1.00 18.98 A ATOM 440 CA TYR A 126 56.516 21.220 7.435 1.00 21.97 A ATOM 441 CB TYR A 126 55.752 22.448 6.933 1.00 25.17 A ATOM 442 CG TYR A 126 56.040 23.690 7.748 1.00 30.98 A ATOM 443 CD1 TYR A 126 55.438 23.886 8.991 1.00 33.95 A ATOM 444 CE1 TYR A 126 55.721 25.015 9.763 1.00 36.60 A ATOM 445 CD2 TYR A 126 56.938 24.657 7.292 1.00 35.43 A ATOM 446 CE2 TYR A 126 57.231 25.792 8.058 1.00 37.20 A ATOM 447 CZ TYR A 126 56.618 25.962 9.291 1.00 37.40 A ATOM 448 OH TYR A 126 56.903 27.073 10.052 1.00 40.85 A ATOM 449 C TYR A 126 55.990 19.956 6.762 1.00 21.35 A ATOM 450 O TYR A 126 55.265 19.175 7.383 1.00 20.49 A ATOM 451 N VAL A 127 56.354 19.746 5.501 1.00 18.16 A ATOM 452 CA VAL A 127 55.892 18.562 4.790 1.00 17.58 A ATOM 453 CB VAL A 127 56.308 18.596 3.308 1.00 17.45 A ATOM 454 CG1 VAL A 127 55.786 17.350 2.600 1.00 17.97 A ATOM 455 CG2 VAL A 127 55.751 19.850 2.641 1.00 14.90 A ATOM 456 C VAL A 127 56.459 17.306 5.448 1.00 18.39 A ATOM 457 O VAL A 127 55.769 16.298 5.583 1.00 18.14 A ATOM 458 N THR A 128 57.716 17.381 5.869 1.00 17.50 A ATOM 459 CA THR A 128 58.375 16.260 6.530 1.00 18.54 A ATOM 460 CB THR A 128 59.861 16.586 6.805 1.00 18.01 A ATOM 461 OG1 THR A 128 60.537 16.804 5.559 1.00 21.14 A ATOM 462 CG2 THR A 128 60.536 15.446 7.545 1.00 17.95 A ATOM 463 C THR A 128 57.676 15.941 7.856 1.00 19.49 A ATOM 464 O THR A 128 57.438 14.776 8.179 1.00 18.76 A ATOM 465 N ARG A 129 57.345 16.981 8.619 1.00 19.60 A ATOM 466 CA ARG A 129 56.673 16.804 9.904 1.00 20.12 A ATOM 467 CB ARG A 129 56.534 18.144 10.621 1.00 21.33 A ATOM 468 CG ARG A 129 55.948 18.029 12.023 1.00 28.02 A ATOM 469 CD ARG A 129 55.721 19.404 12.597 1.00 31.25 A ATOM 470 NE ARG A 129 56.940 20.205 12.560 1.00 37.78 A ATOM 471 CZ ARG A 129 56.962 21.524 12.391 1.00 40.10 A ATOM 472 NH1 ARG A 129 55.828 22.197 12.239 1.00 40.03 A ATOM 473 NH2 ARG A 129 58.119 22.170 12.374 1.00 44.58 A ATOM 474 C ARG A 129 55.288 16.186 9.729 1.00 20.08 A ATOM 475 O ARG A 129 54.891 15.305 10.496 1.00 20.40 A ATOM 476 N GLU A 130 54.553 16.654 8.724 1.00 18.79 A ATOM 477 CA GLU A 130 53.222 16.125 8.454 1.00 20.10 A ATOM 478 CB GLU A 130 52.638 16.749 7.183 1.00 19.92 A ATOM 479 CG GLU A 130 51.350 16.087 6.708 1.00 27.85 A ATOM 480 CD GLU A 130 50.581 16.933 5.707 1.00 29.72 A ATOM 481 OE1 GLU A 130 51.216 17.528 4.814 1.00 33.46 A ATOM 482 OE2 GLU A 130 49.339 16.996 5.807 1.00 30.74 A ATOM 483 C GLU A 130 53.301 14.615 8.295 1.00 19.81 A ATOM 484 O GLU A 130 52.553 13.875 8.935 1.00 18.37 A ATOM 485 N ARG A 131 54.219 14.162 7.447 1.00 20.41 A ATOM 486 CA ARG A 131 54.397 12.735 7.202 1.00 22.45 A ATOM 487 CB ARG A 131 55.442 12.511 6.098 1.00 25.16 A ATOM 488 CG ARG A 131 55.742 11.043 5.840 1.00 28.75 A ATOM 489 CD ARG A 131 56.736 10.837 4.708 1.00 33.75 A ATOM 490 NE ARG A 131 57.020 9.415 4.520 1.00 40.07 A ATOM 491 CZ ARG A 131 57.756 8.915 3.532 1.00 43.07 A ATOM 492 NH1 ARG A 131 58.293 9.721 2.625 1.00 44.91 A ATOM 493 NH2 ARG A 131 57.955 7.606 3.449 1.00 44.45 A ATOM 494 C ARG A 131 54.820 11.982 8.466 1.00 23.24 A ATOM 495 O ARG A 131 54.241 10.948 8.804 1.00 23.86 A ATOM 496 N ASP A 132 55.831 12.497 9.160 1.00 21.99 A ATOM 497 CA ASP A 132 56.318 11.850 10.370 1.00 22.04 A ATOM 498 CB ASP A 132 57.570 12.564 10.888 1.00 23.72 A ATOM 499 CG ASP A 132 58.750 12.442 9.932 1.00 27.77 A ATOM 500 OD1 ASP A 132 58.681 11.620 8.989 1.00 27.34 A ATOM 501 OD2 ASP A 132 59.753 13.163 10.128 1.00 28.70 A ATOM 502 C ASP A 132 55.258 11.772 11.474 1.00 21.69 A ATOM 503 O ASP A 132 55.077 10.723 12.092 1.00 22.75 A ATOM 504 N VAL A 133 54.551 12.868 11.725 1.00 19.54 A ATOM 505 CA VAL A 133 53.525 12.843 12.759 1.00 18.52 A ATOM 506 CB VAL A 133 52.908 14.244 12.990 1.00 19.26 A ATOM 507 CG1 VAL A 133 51.708 14.135 13.918 1.00 18.79 A ATOM 508 CG2 VAL A 133 53.953 15.180 13.604 1.00 18.80 A ATOM 509 C VAL A 133 52.419 11.854 12.398 1.00 19.46 A ATOM 510 O VAL A 133 52.073 10.991 13.200 1.00 19.94 A ATOM 511 N MET A 134 51.878 11.957 11.187 1.00 19.15 A ATOM 512 CA MET A 134 50.807 11.052 10.792 1.00 21.25 A ATOM 513 CB MET A 134 50.309 11.381 9.383 1.00 17.34 A ATOM 514 CG MET A 134 49.615 12.730 9.302 1.00 20.00 A ATOM 515 SD MET A 134 48.643 12.952 7.798 1.00 24.21 A ATOM 516 CE MET A 134 47.033 12.434 8.400 1.00 23.20 A ATOM 517 C MET A 134 51.203 9.582 10.881 1.00 22.43 A ATOM 518 O MET A 134 50.384 8.741 11.249 1.00 23.82 A ATOM 519 N SER A 135 52.454 9.273 10.556 1.00 23.09 A ATOM 520 CA SER A 135 52.939 7.895 10.615 1.00 26.13 A ATOM 521 CB SER A 135 54.356 7.798 10.039 1.00 26.17 A ATOM 522 OG SER A 135 54.383 8.177 8.673 1.00 31.91 A ATOM 523 C SER A 135 52.957 7.358 12.045 1.00 26.58 A ATOM 524 O SER A 135 52.926 6.148 12.261 1.00 26.42 A ATOM 525 N ARG A 136 53.014 8.261 13.018 1.00 25.65 A ATOM 526 CA ARG A 136 53.056 7.870 14.425 1.00 27.47 A ATOM 527 CB ARG A 136 53.823 8.914 15.238 1.00 27.97 A ATOM 528 CG ARG A 136 55.283 9.082 14.857 1.00 32.00 A ATOM 529 CD ARG A 136 55.904 10.218 15.664 1.00 33.03 A ATOM 530 NE ARG A 136 55.602 10.073 17.084 1.00 36.11 A ATOM 531 CZ ARG A 136 55.867 10.990 18.007 1.00 39.74 A ATOM 532 NH1 ARG A 136 56.449 12.132 17.661 1.00 40.55 A ATOM 533 NH2 ARG A 136 55.540 10.769 19.276 1.00 36.72 A ATOM 534 C ARG A 136 51.667 7.709 15.036 1.00 26.38 A ATOM 535 O ARG A 136 51.516 7.121 16.106 1.00 27.06 A ATOM 536 N LEU A 137 50.655 8.235 14.360 1.00 24.77 A ATOM 537 CA LEU A 137 49.294 8.162 14.870 1.00 24.70 A ATOM 538 CB LEU A 137 48.483 9.363 14.371 1.00 24.52 A ATOM 539 CG LEU A 137 49.050 10.760 14.662 1.00 26.67 A ATOM 540 CD1 LEU A 137 48.075 11.813 14.141 1.00 27.25 A ATOM 541 CD2 LEU A 137 49.279 10.945 16.155 1.00 27.09 A ATOM 542 C LEU A 137 48.592 6.868 14.473 1.00 25.20 A ATOM 543 O LEU A 137 48.619 6.469 13.309 1.00 25.99 A ATOM 544 N ASP A 138 47.971 6.218 15.451 1.00 21.89 A ATOM 545 CA ASP A 138 47.239 4.977 15.219 1.00 21.35 A ATOM 546 CB ASP A 138 48.124 3.761 15.523 1.00 22.14 A ATOM 547 CC ASP A 138 47.432 2.448 15.201 1.00 24.90 A ATOM 548 OD1 ASP A 138 46.631 2.423 14.241 1.00 24.78 A ATOM 549 OD2 ASP A 138 47.691 1.443 15.897 1.00 25.39 A ATOM 550 C ASP A 138 46.031 4.991 16.138 1.00 20.47 A ATOM 551 O ASP A 138 45.967 4.248 17.118 1.00 19.06 A ATOM 552 N HIS A 139 45.075 5.852 15.810 1.00 18.27 A ATOM 553 CA HIS A 139 43.869 6.016 16.606 1.00 18.21 A ATOM 554 CB HIS A 139 44.096 7.157 17.612 1.00 15.84 A ATOM 555 CC HIS A 139 42.985 7.332 18.600 1.00 15.24 A ATOM 556 CD2 HIS A 139 42.884 6.964 19.900 1.00 13.97 A ATOM 557 ND1 HIS A 139 41.791 7.943 18.280 1.00 14.74 A ATOM 558 CE1 HIS A 139 41.002 7.944 19.341 1.00 14.19 A ATOM 559 NE2 HIS A 139 41.641 7.356 20.336 1.00 14.15 A ATOM 560 C HIS A 139 42.715 6.330 15.654 1.00 18.50 A ATOM 561 O HIS A 139 42.879 7.080 14.693 1.00 20.80 A ATOM 562 N PRO A 140 41.527 5.767 15.913 1.00 18.32 A ATOM 563 CD PRO A 140 41.143 4.984 17.100 1.00 16.71 A ATOM 564 CA PRO A 140 40.367 6.001 15.048 1.00 17.43 A ATOM 565 CB PRO A 140 39.273 5.157 15.704 1.00 16.64 A ATOM 566 CC PRO A 140 39.643 5.204 17.152 1.00 18.43 A ATOM 567 C PRO A 140 39.914 7.441 14.803 1.00 18.77 A ATOM 568 O PRO A 140 39.207 7.695 13.831 1.00 19.88 A ATOM 569 N PHE A 141 40.301 8.381 15.664 1.00 17.14 A ATOM 570 CA PHE A 141 39.874 9.767 15.477 1.00 16.42 A ATOM 571 CB PHE A 141 39.568 10.422 16.836 1.00 14.60 A ATOM 572 CC PHE A 141 38.386 9.817 17.556 1.00 15.26 A ATOM 573 CD1 PHE A 141 37.335 9.234 16.842 1.00 14.78 A ATOM 574 CD2 PHE A 141 38.297 9.880 18.942 1.00 13.70 A ATOM 575 CE1 PHE A 141 36.215 8.727 17.502 1.00 16.94 A ATOM 576 CE2 PHE A 141 37.178 9.375 19.615 1.00 15.75 A ATOM 577 CZ PHE A 141 36.135 8.799 18.893 1.00 16.89 A ATOM 578 C PHE A 141 40.857 10.641 14.694 1.00 16.15 A ATOM 579 O PHE A 141 40.799 11.871 14.761 1.00 17.35 A ATOM 580 N PHE A 142 41.748 10.011 13.941 1.00 15.88 A ATOM 581 CA PHE A 142 42.727 10.756 13.154 1.00 17.89 A ATOM 582 CB PHE A 142 44.115 10.645 13.793 1.00 17.57 A ATOM 583 CC PHE A 142 44.240 11.371 15.103 1.00 18.74 A ATOM 584 CD1 PHE A 142 44.559 12.726 15.135 1.00 17.77 A ATOM 585 CD2 PHE A 142 43.997 10.711 16.304 1.00 18.74 A ATOM 586 CE1 PHE A 142 44.632 13.417 16.347 1.00 15.77 A ATOM 587 CE2 PHE A 142 44.065 11.393 17.522 1.00 17.56 A ATOM 588 CZ PHE A 142 44.383 12.747 17.542 1.00 17.14 A ATOM 589 C PHE A 142 42.793 10.231 11.729 1.00 19.12 A ATOM 590 O PHE A 142 42.659 9.030 11.504 1.00 20.01 A ATOM 591 N VAL A 143 42.978 11.135 10.769 1.00 18.72 A ATOM 592 CA VAL A 143 43.102 10.735 9.371 1.00 18.52 A ATOM 593 CB VAL A 143 43.294 11.961 8.440 1.00 20.66 A ATOM 594 Cd VAL A 143 43.843 11.521 7.080 1.00 21.29 A ATOM 595 CC2 VAL A 143 41.958 12.673 8.252 1.00 22.97 A ATOM 596 C VAL A 143 44.342 9.865 9.330 1.00 18.68 A ATOM 597 O VAL A 143 45.355 10.199 9.943 1.00 18.42 A ATOM 598 N LYS A 144 44.259 8.745 8.623 1.00 18.30 A ATOM 599 CA LYS A 144 45.384 7.824 8.535 1.00 18.78 A ATOM 600 CB LYS A 144 44.889 6.373 8.608 1.00 22.27 A ATOM 601 CC LYS A 144 46.017 5.340 8.557 1.00 29.72 A ATOM 602 CD LYS A 144 45.491 3.912 8.674 1.00 34.16 A ATOM 603 CE LYS A 144 46.631 2.896 8.577 1.00 37.67 A ATOM 604 NZ LYS A 144 46.138 1.484 8.629 1.00 39.02 A ATOM 605 C LYS A 144 46.192 8.002 7.261 1.00 18.53 A ATOM 606 O LYS A 144 45.643 8.314 6.200 1.00 18.18 A ATOM 607 N LEU A 145 47.502 7.816 7.385 1.00 16.79 A ATOM 608 CA LEU A 145 48.411 7.900 6.251 1.00 17.45 A ATOM 609 CB LEU 145 49.686 8.653 6.641 0.50 18.82 AC1 ATOM 610 CO LEU 145 50.734 8.902 5.549 0.50 20.23 AC1 ATOM 611 CD1 LEU 145 51.836 9.799 6.093 0.50 18.83 AC1 ATOM 612 CD2 LEU 145 51.317 7.581 5.069 0.50 19.79 AC1 ATOM 613 C LEU A 145 48.739 6.450 5.907 1.00 19.19 A ATOM 614 O LEU A 145 49.451 5.772 6.659 1.00 17.36 A ATOM 615 N TYR A 146 48.215 5.972 4.782 1.00 17.28 A ATOM 616 CA TYR A 146 48.444 4.593 4.358 1.00 17.57 A ATOM 617 CB TYR A 146 47.288 4.098 3.486 1.00 17.74 A ATOM 618 CO TYR A 146 45.981 3.926 4.214 1.00 17.50 A ATOM 619 CD1 TYR A 146 45.099 4.995 4.377 1.00 16.50 A ATOM 620 CE1 TYR A 146 43.881 4.827 5.039 1.00 17.10 A ATOM 621 CD2 TYR A 146 45.620 2.686 4.735 1.00 18.28 A ATOM 622 CE2 TYR A 146 44.411 2.506 5.399 1.00 19.84 A ATOM 623 CZ TYR A 146 43.547 3.576 5.544 1.00 17.53 A ATOM 624 OH TYR A 146 42.342 3.376 6.169 1.00 20.67 A ATOM 625 C TYR A 146 49.735 4.376 3.582 1.00 18.72 A ATOM 626 O TYR A 146 50.382 3.338 3.715 1.00 19.51 A ATOM 627 N PHE A 147 50.110 5.350 2.765 1.00 18.09 A ATOM 628 CA PHE A 147 51.307 5.203 1.952 1.00 17.20 A ATOM 629 CB PHE A 147 51.007 4.258 0.783 1.00 16.77 A ATOM 630 CO PHE A 147 49.835 4.699 −0.070 1.00 17.75 A ATOM 631 CD1 PHE A 147 49.967 5.752 −0.975 1.00 16.58 A ATOM 632 CD2 PHE A 147 48.595 4.075 0.053 1.00 18.07 A ATOM 633 CE1 PHE A 147 48.886 6.178 −1.742 1.00 19.62 A ATOM 634 CE2 PHE A 147 47.503 4.492 −0.710 1.00 18.56 A ATOM 635 CZ PHE A 147 47.647 5.546 −1.610 1.00 19.27 A ATOM 636 C PHE A 147 51.768 6.533 1.395 1.00 17.13 A ATOM 637 O PHE A 147 51.045 7.528 1.452 1.00 14.43 A ATOM 638 N THR A 148 52.981 6.534 0.854 1.00 17.12 A ATOM 639 CA THR A 148 53.541 7.718 0.232 1.00 17.96 A ATOM 640 CB THR A 148 54.449 8.531 1.197 1.00 21.51 A ATOM 641 CO1 THR A 148 55.605 7.760 1.537 1.00 18.83 A ATOM 642 CO2 THR A 148 53.700 8.897 2.472 1.00 19.60 A ATOM 643 C THR A 148 54.386 7.262 −0.946 1.00 20.31 A ATOM 644 O THR A 148 54.860 6.124 −0.991 1.00 18.94 A ATOM 645 N PHE A 149 54.543 8.149 −1.916 1.00 19.16 A ATOM 646 CA PHE A 149 55.368 7.877 −3.073 1.00 18.01 A ATOM 647 CB PHE A 149 54.748 6.801 −3.989 1.00 17.23 A ATOM 648 CO PHE A 149 53.389 7.144 −4.544 1.00 16.88 A ATOM 649 CD1 PHE A 149 53.262 7.888 −5.712 1.00 18.58 A ATOM 650 CD2 PHE A 149 52.235 6.668 −3.927 1.00 17.31 A ATOM 651 CE1 PHE A 149 52.007 8.149 −6.267 1.00 19.26 A ATOM 652 CE2 PHE A 149 50.972 6.923 −4.470 1.00 19.17 A ATOM 653 CZ PHE A 149 50.858 7.663 −5.642 1.00 19.60 A ATOM 654 C PHE A 149 55.542 9.205 −3.774 1.00 20.85 A ATOM 655 O PHE A 149 54.934 10.200 −3.376 1.00 19.76 A ATOM 656 N OLN A 150 56.398 9.241 −4.782 1.00 19.79 A ATOM 657 CA OLN A 150 56.636 10.481 −5.497 1.00 24.03 A ATOM 658 CB OLN A 150 57.659 11.347 −4.739 1.00 24.45 A ATOM 659 CO OLN A 150 58.986 10.645 −4.414 1.00 26.28 A ATOM 660 CD OLN A 150 59.988 11.558 −3.692 1.00 29.02 A ATOM 661 OE1 OLN A 150 60.693 12.353 −4.321 1.00 27.05 A ATOM 662 NE2 GIN A 150 60.042 11.449 −2.365 1.00 26.47 A ATOM 663 C GIN A 150 57.160 10.203 −6.885 1.00 23.88 A ATOM 664 O GIN A 150 57.673 9.118 −7.158 1.00 24.79 A ATOM 665 N ASP A 151 56.987 11.171 −7.774 1.00 25.88 A ATOM 666 CA ASP A 151 57.527 11.047 −9.117 1.00 26.49 A ATOM 667 CB ASP A 151 56.437 11.126 −10.199 1.00 24.54 A ATOM 668 CC ASP A 151 55.544 12.336 −10.064 1.00 24.95 A ATOM 669 OD1 ASP A 151 56.005 13.379 −9.561 1.00 22.44 A ATOM 670 OD2 ASP A 151 54.369 12.242 −10.490 1.00 25.72 A ATOM 671 C ASP A 151 58.515 12.203 −9.220 1.00 28.63 A ATOM 672 O ASP A 151 58.890 12.780 −8.194 1.00 27.83 A ATOM 673 N ASP A 152 58.934 12.560 −10.426 1.00 29.21 A ATOM 674 CA ASP A 152 59.907 13.636 −10.562 1.00 31.88 A ATOM 675 CB ASP A 152 60.325 13.792 −12.026 1.00 33.94 A ATOM 676 CC ASP A 152 61.033 12.564 −12.557 1.00 38.88 A ATOM 677 OD1 ASP A 152 61.817 11.959 −11.791 1.00 39.67 A ATOM 678 OD2 ASP A 152 60.817 12.211 −13.738 1.00 41.57 A ATOM 679 C ASP A 152 59.487 14.994 −10.013 1.00 30.90 A ATOM 680 O ASP A 152 60.316 15.735 −9.482 1.00 31.69 A ATOM 681 N CLU A 153 58.207 15.322 −10.107 1.00 29.44 A ATOM 682 CA CLU A 153 57.767 16.632 −9.646 1.00 28.69 A ATOM 683 CB CLU A 153 56.984 17.327 −10.766 1.00 32.90 A ATOM 684 CC CLU A 153 57.451 16.987 −12.183 1.00 40.57 A ATOM 685 CD CLU A 153 56.920 15.643 −12.675 1.00 45.78 A ATOM 686 OE1 CLU A 153 55.682 15.482 −12.760 1.00 48.91 A ATOM 687 0E2 CLU A 153 57.736 14.747 −12.979 1.00 48.95 A ATOM 688 C CLU A 153 56.929 16.683 −8.372 1.00 26.43 A ATOM 689 O CLU A 153 56.947 17.688 −7.660 1.00 25.08 A ATOM 690 N LYS A 154 56.205 15.610 −8.069 1.00 22.39 A ATOM 691 CA LYS A 154 55.318 15.631 −6.912 1.00 21.43 A ATOM 692 CB LYS A 154 53.861 15.628 −7.398 1.00 20.33 A ATOM 693 CC LYS A 154 53.505 16.716 −8.403 1.00 21.92 A ATOM 694 CD LYS A 154 52.211 16.375 −9.146 1.00 19.70 A ATOM 695 CE LYS A 154 51.775 17.503 −10.077 1.00 20.04 A ATOM 696 NZ LYS A 154 50.631 17.094 −10.951 1.00 19.97 A ATOM 697 C LYS A 154 55.458 14.522 −5.881 1.00 20.43 A ATOM 698 O LYS A 154 55.949 13.426 −6.173 1.00 21.13 A ATOM 699 N LEU A 155 54.985 14.832 −4.676 1.00 19.69 A ATOM 700 CA LEU A 155 54.950 13.900 −3.553 1.00 19.10 A ATOM 701 CB LEU 155 55.362 14.588 −2.252 1.00 19.65 A ATOM 702 CC LEU A 155 56.740 15.234 −2.129 1.00 21.20 A ATOM 703 CD1 LEU A 155 56.848 15.918 −0.770 1.00 23.42 A ATOM 704 CD2 LEU A 155 57.816 14.174 −2.277 1.00 23.08 A ATOM 705 C LEU A 155 53.478 13.507 −3.427 1.00 18.87 A ATOM 706 O LEU A 155 52.600 14.348 −3.620 1.00 18.61 A ATOM 707 N TYR A 156 53.209 12.249 −3.091 1.00 15.02 A ATOM 708 CA TYR A 156 51.834 11.783 −2.934 1.00 16.29 A ATOM 709 CB TYR A 156 51.470 10.769 −4.029 1.00 14.20 A ATOM 710 CC TYR A 156 51.603 11.273 −5.449 1.00 17.29 A ATOM 711 CD1 TYR A 156 52.857 11.429 −6.045 1.00 16.46 A ATOM 712 CEl TYR A 156 52.978 11.884 −7.360 1.00 18.68 A ATOM 713 CD2 TYR A 156 50.474 11.588 −6.202 1.00 16.43 A ATOM 714 CE2 TYR A 156 50.583 12.048 −7.512 1.00 16.31 A ATOM 715 CZ TYR A 156 51.835 12.192 −8.083 1.00 18.17 A ATOM 716 OH TYR A 156 51.941 12.651 −9.371 1.00 17.47 A ATOM 717 C TYR A 156 51.657 11.108 −1.572 1.00 16.32 A ATOM 718 O TYR A 156 52.412 10.197 −1.235 1.00 16.27 A ATOM 719 N PHE A 157 50.678 11.568 −0.792 1.00 15.47 A ATOM 720 CA PHE A 157 50.385 10.966 0.508 1.00 16.66 A ATOM 721 CB PHE A 157 50.324 12.014 1.629 1.00 16.91 A ATOM 722 CG PHE A 157 51.631 12.708 1.907 1.00 18.96 A ATOM 723 CD1 PHE A 157 52.821 12.261 1.340 1.00 20.31 A ATOM 724 CD2 PHE A 157 51.664 13.829 2.732 1.00 21.12 A ATOM 725 CE1 PHE A 157 54.025 12.926 1.585 1.00 22.08 A ATOM 726 CE2 PHE A 157 52.865 14.500 2.982 1.00 22.18 A ATOM 727 CZ PHE A 157 54.045 14.045 2.405 1.00 21.27 A ATOM 728 C PHE A 157 49.016 10.308 0.404 1.00 16.52 A ATOM 729 O PHE A 157 48.029 10.979 0.110 1.00 17.32 A ATOM 730 N GLY A 158 48.953 9.002 0.644 1.00 15.97 A ATOM 731 CA GLY A 158 47.684 8.299 0.572 1.00 16.13 A ATOM 732 C GLY A 158 47.000 8.383 1.920 1.00 14.94 A ATOM 733 O GLY A 158 47.445 7.756 2.879 1.00 16.28 A ATOM 734 N LEU A 159 45.915 9.145 1.989 1.00 13.50 A ATOM 735 CA LEU A 159 45.191 9.340 3.241 1.00 15.20 A ATOM 736 CB LEU A 159 45.031 10.835 3.517 1.00 14.20 A ATOM 737 CG LEU A 159 46.270 11.726 3.385 1.00 19.00 A ATOM 738 CD1 LEU A 159 45.847 13.188 3.477 1.00 17.12 A ATOM 739 CD2 LEU A 159 47.275 11.390 4.471 1.00 14.71 A ATOM 740 C LEU A 159 43.809 8.716 3.232 1.00 15.53 A ATOM 741 O LEU A 159 43.232 8.472 2.177 1.00 16.05 A ATOM 742 N SER A 160 43.268 8.469 4.418 1.00 15.86 A ATOM 743 CA SER A 160 41.932 7.917 4.498 1.00 19.01 A ATOM 744 CB SER A 160 41.566 7.582 5.949 1.00 22.90 A ATOM 745 OG SER A 160 41.901 8.629 6.833 1.00 24.18 A ATOM 746 C SER A 160 40.987 8.968 3.924 1.00 20.43 A ATOM 747 O SER A 160 41.213 10.173 4.062 1.00 19.96 A ATOM 748 N TYR A 161 39.945 8.508 3.250 1.00 19.20 A ATOM 749 CA TYR A 161 38.975 9.406 2.644 1.00 20.37 A ATOM 750 CB TYR A 161 38.471 8.785 1.332 1.00 20.00 A ATOM 751 CG TYR A 161 37.314 9.502 0.666 1.00 20.72 A ATOM 752 CD1 TYR A 161 37.222 10.895 0.682 1.00 18.22 A ATOM 753 CE1 TYR A 161 36.180 11.557 0.029 1.00 22.24 A ATOM 754 CD2 TYR A 161 36.333 8.784 −0.020 1.00 20.53 A ATOM 755 CE2 TYR A 161 35.287 9.436 −0.678 1.00 24.24 A ATOM 756 CZ TYR A 161 35.218 10.822 −0.648 1.00 22.32 A ATOM 757 OH TYR A 161 34.194 11.471 −1.298 1.00 23.03 A ATOM 758 C TYR A 161 37.812 9.681 3.598 1.00 20.14 A ATOM 759 O TYR A 161 36.959 8.819 3.810 1.00 19.53 A ATOM 760 N ALA A 162 37.791 10.880 4.178 1.00 19.92 A ATOM 761 CA ALA A 162 36.721 11.271 5.099 1.00 21.07 A ATOM 762 CB ALA A 162 37.187 12.419 6.002 1.00 19.60 A ATOM 763 C ALA A 162 35.542 11.712 4.238 1.00 22.07 A ATOM 764 O ALA A 162 35.436 12.875 3.860 1.00 20.66 A ATOM 765 N LYS A 163 34.653 10.769 3.945 1.00 23.27 A ATOM 766 CA LYS A 163 33.503 11.017 3.080 1.00 27.12 A ATOM 767 CB LYS A 163 32.663 9.741 2.963 1.00 29.68 A ATOM 768 CG LYS A 163 33.455 8.524 2.515 1.00 37.67 A ATOM 769 CD LYS A 163 32.556 7.310 2.321 1.00 42.24 A ATOM 770 CE LYS A 163 33.373 6.034 2.185 1.00 44.48 A ATOM 771 NZ LYS A 163 34.143 5.735 3.430 1.00 44.88 A ATOM 772 C LYS A 163 32.581 12.186 3.411 1.00 25.78 A ATOM 773 O LYS A 163 32.103 12.863 2.506 1.00 26.53 A ATOM 774 N ASN A 164 32.327 12.441 4.689 1.00 24.57 A ATOM 775 CA ASN A 164 31.420 13.522 5.033 1.00 23.77 A ATOM 776 CB ASN A 164 30.610 13.129 6.265 1.00 25.02 A ATOM 777 CG ASN A 164 29.537 12.101 5.932 1.00 27.54 A ATOM 778 OD1 ASN A 164 28.772 12.281 4.983 1.00 28.79 A ATOM 779 ND2 ASN A 164 29.475 11.024 6.704 1.00 27.13 A ATOM 780 C ASN A 164 31.999 14.931 5.169 1.00 24.43 A ATOM 781 O ASN A 164 31.306 15.856 5.589 1.00 23.98 A ATOM 782 N GLY A 165 33.262 15.097 4.795 1.00 21.56 A ATOM 783 CA GLY A 165 33.873 16.414 4.836 1.00 24.39 A ATOM 784 C GLY A 165 34.191 17.043 6.181 1.00 23.62 A ATOM 785 O GLY A 165 34.380 16.352 7.177 1.00 23.26 A ATOM 786 N GLU A 166 34.234 18.373 6.186 1.00 23.22 A ATOM 787 CA GLU A 166 34.563 19.176 7.362 1.00 24.54 A ATOM 788 CB GLU A 166 35.055 20.558 6.913 1.00 25.04 A ATOM 789 CG GLU A 166 36.419 20.569 6.229 1.00 26.48 A ATOM 790 CD GLU A 166 36.699 21.889 5.517 1.00 30.02 A ATOM 791 OE1 GLU A 166 36.081 22.906 5.889 1.00 29.33 A ATOM 792 0E2 GLU A 166 37.544 21.916 4.596 1.00 30.48 A ATOM 793 C GLU A 166 33.436 19.372 8.369 1.00 24.44 A ATOM 794 O GLU A 166 32.279 19.541 8.001 1.00 22.76 A ATOM 795 N LEU A 167 33.791 19.370 9.649 1.00 22.95 A ATOM 796 CA LEU A 167 32.813 19.581 10.707 1.00 22.26 A ATOM 797 CB LEU A 167 33.497 19.481 12.073 1.00 22.32 A ATOM 798 CG LEU A 167 32.706 19.923 13.306 1.00 22.04 A ATOM 799 CD1 LEU A 167 31.454 19.074 13.463 1.00 19.66 A ATOM 800 CD2 LEU A 167 33.597 19.805 14.537 1.00 21.17 A ATOM 801 C LEU A 167 32.193 20.971 10.529 1.00 23.49 A ATOM 802 O LEU A 167 31.047 21.209 10.907 1.00 23.56 A ATOM 803 N LEU A 168 32.960 21.887 9.948 1.00 24.25 A ATOM 804 CA LEU A 168 32.473 23.245 9.722 1.00 26.64 A ATOM 805 CB LEU A 168 33.560 24.099 9.066 1.00 25.62 A ATOM 806 CG LEU A 168 33.198 25.546 8.707 1.00 27.34 A ATOM 807 CD1 LEU A 168 32.718 26.296 9.946 1.00 26.42 A ATOM 808 CD2 LEU A 168 34.418 26.238 8.119 1.00 26.74 A ATOM 809 C LEU A 168 31.234 23.218 8.829 1.00 27.13 A ATOM 810 O LEU A 168 30.297 23.989 9.030 1.00 26.01 A ATOM 811 N LYS A 169 31.233 22.320 7.848 1.00 26.41 A ATOM 812 CA LYS A 169 30.106 22.210 6.934 1.00 27.70 A ATOM 813 CB LYS A 169 30.324 21.064 5.945 1.00 30.49 A ATOM 814 CG LYS A 169 29.151 20.854 4.993 1.00 32.47 A ATOM 815 CD LYS A 169 29.407 19.728 3.998 1.00 35.98 A ATOM 816 CE LYS A 169 29.462 18.372 4.683 1.00 38.53 A ATOM 817 NZ LYS A 169 29.622 17.263 3.702 1.00 41.00 A ATOM 818 C LYS A 169 28.801 21.985 7.682 1.00 28.12 A ATOM 819 O LYS A 169 27.785 22.608 7.371 1.00 28.08 A ATOM 820 N TYR A 170 28.826 21.094 8.668 1.00 26.53 A ATOM 821 CA TYR A 170 27.624 20.791 9.434 1.00 26.95 A ATOM 822 CB TYR A 170 27.810 19.476 10.193 1.00 25.03 A ATOM 823 CG TYR A 170 27.898 18.300 9.251 1.00 26.65 A ATOM 824 CD1 TYR A 170 26.745 17.661 8.790 1.00 28.27 A ATOM 825 CE1 TYR A 170 26.814 16.642 7.839 1.00 26.85 A ATOM 826 CD2 TYR A 170 29.127 17.884 8.742 1.00 27.83 A ATOM 827 CE2 TYR A 170 29.209 16.869 7.792 1.00 27.19 A ATOM 828 CZ TYR A 170 28.049 16.254 7.343 1.00 30.02 A ATOM 829 OH TYR A 170 28.130 15.268 6.382 1.00 29.23 A ATOM 830 C TYR A 170 27.229 21.918 10.376 1.00 27.59 A ATOM 831 O TYR A 170 26.045 22.122 10.642 1.00 29.25 A ATOM 832 N ILE A 171 28.208 22.660 10.882 1.00 28.16 A ATOM 833 CA ILE A 171 27.883 23.770 11.763 1.00 29.03 A ATOM 834 CB ILE A 171 29.151 24.435 12.337 1.00 27.51 A ATOM 835 CG2 ILE A 171 28.773 25.705 13.084 1.00 27.97 A ATOM 836 CG1 ILE A 171 29.872 23.458 13.272 1.00 26.70 A ATOM 837 CD1 ILE A 171 31.163 23.996 13.856 1.00 24.07 A ATOM 838 C ILE A 171 27.094 24.796 10.944 1.00 31.41 A ATOM 839 O ILE A 171 26.088 25.335 11.407 1.00 31.69 A ATOM 840 N ARG A 172 27.546 25.047 9.719 1.00 33.21 A ATOM 841 CA ARG A 172 26.874 26.000 8.844 1.00 36.54 A ATOM 842 CB ARG A 172 27.734 26.314 7.616 1.00 37.73 A ATOM 843 CG ARG A 172 29.057 27.011 7.912 1.00 41.65 A ATOM 844 CD ARG A 172 29.708 27.492 6.616 1.00 45.29 A ATOM 845 NE ARG A 172 31.037 28.070 6.812 1.00 48.51 A ATOM 846 CZ ARG A 172 31.314 29.059 7.658 1.00 51.53 A ATOM 847 NH1 ARG A 172 30.355 29.593 8.406 1.00 53.75 A ATOM 848 NH2 ARG A 172 32.553 29.526 7.748 1.00 51.21 A ATOM 849 C ARG A 172 25.528 25.459 8.378 1.00 37.67 A ATOM 850 O ARG A 172 24.550 26.200 8.288 1.00 39.09 A ATOM 851 N LYS A 173 25.481 24.163 8.092 1.00 38.44 A ATOM 852 CA LYS A 173 24.259 23.528 7.619 1.00 39.25 A ATOM 853 CB LYS A 173 24.523 22.061 7.272 1.00 41.89 A ATOM 854 CG LYS A 173 23.279 21.298 6.830 1.00 45.52 A ATOM 855 CD LYS A 173 23.557 19.808 6.653 1.00 49.60 A ATOM 856 CE LYS A 173 24.477 19.530 5.469 1.00 52.63 A ATOM 857 NZ LYS A 173 23.855 19.894 4.160 1.00 54.61 A ATOM 858 C LYS A 173 23.089 23.608 8.595 1.00 39.30 A ATOM 859 O LYS A 173 21.981 23.960 8.201 1.00 39.62 A ATOM 860 N ILE A 174 23.320 23.282 9.863 1.00 37.96 A ATOM 861 CA ILE A 174 22.229 23.314 10.833 1.00 37.36 A ATOM 862 CB ILE A 174 22.159 21.998 11.652 1.00 37.44 A ATOM 863 CG2 ILE A 174 22.058 20.802 10.709 1.00 38.37 A ATOM 864 CG1 ILE A 174 23.397 21.850 12.532 1.00 37.25 A ATOM 865 CD1 ILE A 174 23.355 20.620 13.418 1.00 36.85 A ATOM 866 C ILE A 174 22.259 24.492 11.801 1.00 36.71 A ATOM 867 O ILE A 174 21.448 24.556 12.724 1.00 38.05 A ATOM 868 N GLY A 175 23.185 25.423 11.592 1.00 35.48 A ATOM 869 CA GLY A 175 23.265 26.585 12.462 1.00 35.29 A ATOM 870 C GLY A 175 24.053 26.360 13.737 1.00 35.06 A ATOM 871 O GLY A 175 25.066 27.019 13.970 1.00 37.46 A ATOM 872 N SER A 176 23.581 25.441 14.571 1.00 33.94 A ATOM 873 CA SER A 176 24.253 25.113 15.822 1.00 32.84 A ATOM 874 CB SER A 176 23.938 26.155 16.901 1.00 33.54 A ATOM 875 OG SER A 176 22.599 26.056 17.347 1.00 34.86 A ATOM 876 C SER A 176 23.796 23.731 16.276 1.00 32.34 A ATOM 877 O SER A 176 22.726 23.263 15.884 1.00 32.82 A ATOM 878 N PHE A 177 24.609 23.085 17.103 1.00 29.39 A ATOM 879 CA PHE A 177 24.313 21.743 17.597 1.00 27.20 A ATOM 880 CB PHE A 177 25.621 20.989 17.865 1.00 26.39 A ATOM 881 CG PHE A 177 26.372 20.585 16.622 1.00 26.18 A ATOM 882 CD1 PHE A 177 26.210 21.277 15.426 1.00 25.30 A ATOM 883 CD2 PHE A 177 27.266 19.516 16.662 1.00 26.05 A ATOM 884 CE1 PHE A 177 26.923 20.912 14.290 1.00 26.59 A ATOM 885 CE2 PHE A 177 27.986 19.143 15.532 1.00 26.06 A ATOM 886 CZ PHE A 177 27.815 19.841 14.343 1.00 25.42 A ATOM 887 C PHE A 177 23.500 21.752 18.884 1.00 27.00 A ATOM 888 O PHE A 177 23.704 22.610 19.747 1.00 26.48 A ATOM 889 N ASP A 178 22.578 20.802 19.022 1.00 26.70 A ATOM 890 CA ASP A 178 21.816 20.729 20.260 1.00 26.35 A ATOM 891 CB ASP A 178 20.621 19.773 20.142 1.00 29.90 A ATOM 892 CG ASP A 178 21.020 18.372 19.720 1.00 32.28 A ATOM 893 OD1 ASP A 178 22.157 17.949 20.014 1.00 35.21 A ATOM 894 0D2 ASP A 178 20.179 17.683 19.105 1.00 34.79 A ATOM 895 C ASP A 178 22.810 20.228 21.311 1.00 25.03 A ATOM 896 O ASP A 178 23.974 19.968 20.992 1.00 21.24 A ATOM 897 N GLU A 179 22.361 20.083 22.552 1.00 23.60 A ATOM 898 CA GLU A 179 23.247 19.644 23.619 1.00 25.18 A ATOM 899 CB GLU A 179 22.542 19.770 24.971 1.00 27.60 A ATOM 900 CC GLU A 179 23.324 19.176 26.130 1.00 32.58 A ATOM 901 CD GLU A 179 22.997 19.845 27.449 1.00 35.82 A ATOM 902 OE1 GLU A 179 21.825 20.224 27.645 1.00 35.95 A ATOM 903 OE2 GLU A 179 23.912 19.984 28.291 1.00 38.19 A ATOM 904 C GLU A 179 23.808 18.235 23.450 1.00 24.08 A ATOM 905 O GLU A 179 24.977 17.989 23.756 1.00 22.79 A ATOM 906 N THR A 180 22.983 17.316 22.961 1.00 23.36 A ATOM 907 CA THR A 180 23.412 15.935 22.761 1.00 22.15 A ATOM 908 CB THR A 180 22.224 15.054 22.320 1.00 23.77 A ATOM 909 OG1 THR A 180 21.222 15.075 23.341 1.00 26.37 A ATOM 910 CC2 THR A 180 22.670 13.616 22.088 1.00 22.66 A ATOM 911 C THR A 180 24.533 15.830 21.724 1.00 22.01 A ATOM 912 O THR A 180 25.533 15.141 21.944 1.00 19.87 A ATOM 913 N CYS A 181 24.365 16.511 20.596 1.00 21.21 A ATOM 914 CA CYS A 181 25.372 16.480 19.541 1.00 22.22 A ATOM 915 CB CYS A 181 24.800 17.065 18.250 1.00 24.62 A ATOM 916 SC CYS A 181 23.435 16.080 17.560 1.00 29.50 A ATOM 917 C CYS A 181 26.633 17.232 19.954 1.00 23.07 A ATOM 918 O CYS A 181 27.746 16.827 19.608 1.00 23.95 A ATOM 919 N THR A 182 26.463 18.325 20.695 1.00 22.76 A ATOM 920 CA THR A 182 27.606 19.103 21.161 1.00 21.49 A ATOM 921 CB THR A 182 27.167 20.346 21.978 1.00 21.37 A ATOM 922 OG1 THR A 182 26.459 21.262 21.134 1.00 22.50 A ATOM 923 CG2 THR A 182 28.379 21.046 22.565 1.00 18.36 A ATOM 924 C THR A 182 28.454 18.215 22.071 1.00 21.48 A ATOM 925 O THR A 182 29.669 18.090 21.894 1.00 19.95 A ATOM 926 N ARC A 183 27.798 17.602 23.050 1.00 18.97 A ATOM 927 CA ARC A 183 28.468 16.723 23.996 1.00 19.39 A ATOM 928 CB ARC 183 27.455 16.140 24.984 0.50 19.46 AC1 ATOM 929 CC ARC 183 28.030 15.062 25.887 0.50 18.77 AC1 ATOM 930 CD ARC 183 27.021 14.571 26.925 0.50 21.19 AC1 ATOM 931 NE ARC 183 26.605 15.642 27.824 0.50 19.46 AC1 ATOM 932 CZ ARC 183 25.496 16.362 27.679 0.50 20.45 AC1 ATOM 933 NH1 ARC 183 24.672 16.123 26.666 0.50 19.81 AC1 ATOM 934 NH2 ARC 183 25.224 17.338 28.539 0.50 17.11 AC1 ATOM 935 C ARC A 183 29.206 15.577 23.302 1.00 20.02 A ATOM 936 O ARC A 183 30.383 15.333 23.573 1.00 19.97 A ATOM 937 N PHE A 184 28.520 14.871 22.409 1.00 19.24 A ATOM 938 CA PHE A 184 29.144 13.746 21.722 1.00 18.04 A ATOM 939 CB PHE A 184 28.158 13.078 20.764 1.00 21.05 A ATOM 940 CC PHE A 184 28.719 11.857 20.098 1.00 22.67 A ATOM 941 CD1 PHE A 184 28.717 10.630 20.754 1.00 22.97 A ATOM 942 CD2 PHE A 184 29.317 11.949 18.850 1.00 19.97 A ATOM 943 CE1 PHE A 184 29.308 9.510 20.176 1.00 23.53 A ATOM 944 CE2 PHE A 184 29.915 10.833 18.263 1.00 24.11 A ATOM 945 CZ PHE A 184 29.910 9.613 18.928 1.00 22.97 A ATOM 946 C PHE A 184 30.403 14.127 20.941 1.00 17.99 A ATOM 947 O PHE A 184 31.461 13.531 21.130 1.00 18.89 A ATOM 948 N TYR A 185 30.292 15.110 20.056 1.00 15.73 A ATOM 949 CA TYR A 185 31.443 15.519 19.265 1.00 15.72 A ATOM 950 CB TYR A 185 30.992 16.413 18.111 1.00 17.33 A ATOM 951 CC TYR A 185 30.364 15.584 17.015 1.00 19.37 A ATOM 952 CD1 TYR A 185 31.159 14.809 16.168 1.00 16.53 A ATOM 953 CE1 TYR A 185 30.590 13.952 15.232 1.00 18.12 A ATOM 954 CD2 TYR A 185 28.976 15.484 16.892 1.00 18.18 A ATOM 955 CE2 TYR A 185 28.398 14.623 15.956 1.00 18.90 A ATOM 956 CZ TYR A 185 29.211 13.861 15.133 1.00 18.41 A ATOM 957 OH TYR A 185 28.650 12.995 14.218 1.00 20.48 A ATOM 958 C TYR A 185 32.544 16.172 20.083 1.00 15.79 A ATOM 959 O TYR A 185 33.720 16.015 19.766 1.00 17.69 A ATOM 960 N THR A 186 32.176 16.887 21.142 1.00 15.68 A ATOM 961 CA THR A 186 33.184 17.504 21.997 1.00 16.03 A ATOM 962 CB THR A 186 32.559 18.403 23.094 1.00 16.62 A ATOM 963 OG1 THR A 186 31.866 19.503 22.481 1.00 14.79 A ATOM 964 CO2 THR A 186 33.656 18.953 24.019 1.00 14.68 A ATOM 965 C THR A 186 33.954 16.375 22.680 1.00 15.59 A ATOM 966 O THR A 186 35.176 16.443 22.823 1.00 13.77 A ATOM 967 N ALA A 187 33.234 15.333 23.097 1.00 14.06 A ATOM 968 CA ALA A 187 33.869 14.196 23.757 1.00 14.74 A ATOM 969 CB ALA A 187 32.810 13.195 24.224 1.00 14.32 A ATOM 970 C ALA A 187 34.875 13.509 22.821 1.00 14.41 A ATOM 971 O ALA A 187 35.972 13.136 23.247 1.00 15.61 A ATOM 972 N GLU A 188 34.516 13.340 21.549 1.00 14.01 A ATOM 973 CA GLU A 188 35.443 12.704 20.615 1.00 13.50 A ATOM 974 CB GLU A 188 34.782 12.449 19.251 1.00 12.85 A ATOM 975 CO GLU A 188 33.622 11.454 19.282 1.00 12.71 A ATOM 976 CD GLU A 188 33.464 10.685 17.979 1.00 15.01 A ATOM 977 OE1 GLU A 188 33.687 11.275 16.899 1.00 13.21 A ATOM 978 OE2 GLU A 188 33.110 9.484 18.031 1.00 17.69 A ATOM 979 C GLU A 188 36.682 13.582 20.436 1.00 13.34 A ATOM 980 O GLU A 188 37.803 13.085 20.408 1.00 14.69 A ATOM 981 N ILE A 189 36.486 14.893 20.326 1.00 13.52 A ATOM 982 CA ILE A 189 37.627 15.787 20.159 1.00 13.35 A ATOM 983 CB ILE A 189 37.169 17.247 19.939 1.00 13.95 A ATOM 984 CO2 ILE A 189 38.381 18.165 19.822 1.00 12.47 A ATOM 985 CCI ILE A 189 36.302 17.332 18.671 1.00 13.44 A ATOM 986 CD1 ILE A 189 35.588 18.664 18.491 1.00 14.29 A ATOM 987 C ILE A 189 38.530 15.702 21.394 1.00 14.63 A ATOM 988 O ILE A 189 39.753 15.595 21.271 1.00 12.97 A ATOM 989 N VAL A 190 37.927 15.751 22.582 1.00 14.35 A ATOM 990 CA VAL A 190 38.684 15.655 23.832 1.00 13.22 A ATOM 991 CB VAL A 190 37.743 15.690 25.061 1.00 14.28 A ATOM 992 CCI VAL A 190 38.509 15.267 26.326 1.00 15.08 A ATOM 993 C02 VAL A 190 37.160 17.082 25.233 1.00 12.08 A ATOM 994 C VAL A 190 39.468 14.338 23.859 1.00 14.61 A ATOM 995 O VAL A 190 40.634 14.304 24.250 1.00 13.72 A ATOM 996 N SER A 191 38.825 13.254 23.432 1.00 15.26 A ATOM 997 CA SER A 191 39.478 11.943 23.421 1.00 16.81 A ATOM 998 CB SER 191 38.470 10.857 23.041 0.50 16.14 AC1 ATOM 999 OG SER 191 39.018 9.569 23.238 0.50 16.94 AC1 ATOM 1000 C SER A 191 40.649 11.928 22.441 1.00 16.58 A ATOM 1001 O SER A 191 41.697 11.335 22.713 1.00 13.96 A ATOM 1002 N ALA A 192 40.468 12.586 21.300 1.00 15.26 A ATOM 1003 CA ALA A 192 41.518 12.645 20.292 1.00 14.37 A ATOM 1004 CB ALA A 192 40.989 13.296 19.016 1.00 14.43 A ATOM 1005 C ALA A 192 42.695 13.440 20.845 1.00 16.46 A ATOM 1006 O ALA A 192 43.851 13.038 20.697 1.00 17.96 A ATOM 1007 N LEU A 193 42.401 14.563 21.496 1.00 15.02 A ATOM 1008 CA LEU A 193 43.459 15.392 22.067 1.00 15.42 A ATOM 1009 CB LEU A 193 42.884 16.712 22.600 1.00 12.88 A ATOM 1010 CO LEU A 193 42.445 17.721 21.525 1.00 15.97 A ATOM 1011 CD1 LEU A 193 41.869 18.979 22.190 1.00 13.97 A ATOM 1012 CD2 LEU A 193 43.642 18.088 20.655 1.00 14.58 A ATOM 1013 C LEU A 193 44.211 14.659 23.174 1.00 14.49 A ATOM 1014 O LEU A 193 45.427 14.813 23.310 1.00 16.56 A ATOM 1015 N OLU A 194 43.500 13.870 23.975 1.00 13.96 A ATOM 1016 CA GLU A 194 44.179 13.123 25.032 1.00 14.08 A ATOM 1017 CB GLU A 194 43.190 12.295 25.857 1.00 14.65 A ATOM 1018 CC GLU A 194 43.882 11.301 26.789 1.00 17.09 A ATOM 1019 CD GLU A 194 42.924 10.592 27.730 1.00 19.59 A ATOM 1020 OE1 GLU A 194 41.809 10.237 27.295 1.00 19.25 A ATOM 1021 OE2 GLU A 194 43.302 10.380 28.906 1.00 20.20 A ATOM 1022 C GLU A 194 45.208 12.199 24.386 1.00 13.57 A ATOM 1023 O GLU A 194 46.337 12.093 24.847 1.00 14.23 A ATOM 1024 N TYR A 195 44.822 11.544 23.301 1.00 14.89 A ATOM 1025 CA TYR A 195 45.743 10.642 22.618 1.00 16.58 A ATOM 1026 CB TYR A 195 45.030 9.910 21.488 1.00 17.29 A ATOM 1027 CC TYR A 195 45.956 9.058 20.649 1.00 17.92 A ATOM 1028 CD1 TYR A 195 46.347 7.788 21.077 1.00 17.96 A ATOM 1029 CE1 TYR A 195 47.203 6.996 20.304 1.00 19.77 A ATOM 1030 CD2 TYR A 195 46.445 9.524 19.428 1.00 16.67 A ATOM 1031 CE2 TYR A 195 47.299 8.744 18.650 1.00 18.51 A ATOM 1032 CZ TYR A 195 47.671 7.481 19.094 1.00 20.24 A ATOM 1033 OH TYR A 195 48.506 6.705 18.325 1.00 21.89 A ATOM 1034 C TYR A 195 46.917 11.419 22.035 1.00 16.98 A ATOM 1035 O TYR A 195 48.081 11.047 22.203 1.00 14.61 A ATOM 1036 N LEU A 196 46.599 12.507 21.347 1.00 16.30 A ATOM 1037 CA LEU A 196 47.619 13.328 20.720 1.00 18.15 A ATOM 1038 CB LEU A 196 46.969 14.502 19.982 1.00 18.59 A ATOM 1039 CC LEU A 196 47.834 15.203 18.935 1.00 22.51 A ATOM 1040 CD1 LEU A 196 48.222 14.206 17.841 1.00 20.94 A ATOM 1041 CD2 LEU A 196 47.060 16.375 18.338 1.00 22.98 A ATOM 1042 C LEU A 196 48.592 13.844 21.763 1.00 17.75 A ATOM 1043 O LEU A 196 49.801 13.644 21.649 1.00 18.33 A ATOM 1044 N HIS A 197 48.064 14.495 22.792 1.00 17.12 A ATOM 1045 CA HIS A 197 48.913 15.042 23.842 1.00 18.47 A ATOM 1046 CB HIS A 197 48.069 15.866 24.817 1.00 15.90 A ATOM 1047 CC HIS A 197 47.571 17.152 24.231 1.00 19.15 A ATOM 1048 CD2 HIS A 197 47.830 17.745 23.038 1.00 18.22 A ATOM 1049 ND1 HIS A 197 46.704 17.992 24.897 1.00 17.47 A ATOM 1050 CE HIS A 197 46.450 19.047 24.139 1.00 19.74 A ATOM 1051 NE2 HIS A 197 47.119 18.921 23.007 1.00 15.69 A ATOM 1052 C HIS A 197 49.696 13.958 24.572 1.00 19.40 A ATOM 1053 O HIS A 197 50.823 14.192 25.021 1.00 19.42 A ATOM 1054 N GLY A 198 49.106 12.770 24.679 1.00 18.59 A ATOM 1055 CA GLY A 198 49.793 11.675 25.339 1.00 19.60 A ATOM 1056 C GLY A 198 51.075 11.307 24.612 1.00 21.86 A ATOM 1057 O GLY A 198 51.963 10.682 25.186 1.00 23.09 A ATOM 1058 N LYS A 199 51.174 11.687 23.341 1.00 22.81 A ATOM 1059 CA LYS A 199 52.368 11.401 22.549 1.00 24.43 A ATOM 1060 CB LYS A 199 51.990 10.905 21.154 1.00 26.00 A ATOM 1061 CC LYS A 199 51.378 9.520 21.133 1.00 30.98 A ATOM 1062 CD LYS A 199 51.291 9.002 19.708 1.00 36.85 A ATOM 1063 CE LYS A 199 50.832 7.559 19.682 1.00 40.37 A ATOM 1064 NZ LYS A 199 51.646 6.691 20.581 1.00 43.48 A ATOM 1065 C LYS A 199 53.253 12.631 22.414 1.00 23.88 A ATOM 1066 O LYS A 199 54.144 12.669 21.568 1.00 24.97 A ATOM 1067 N GLY A 200 52.997 13.638 23.243 1.00 24.00 A ATOM 1068 CA GLY A 200 53.790 14.853 23.203 1.00 22.12 A ATOM 1069 C GLY A 200 53.665 15.632 21.907 1.00 22.14 A ATOM 1070 O GLY A 200 54.632 16.231 21.439 1.00 22.41 A ATOM 1071 N ILE A 201 52.475 15.630 21.320 1.00 20.00 A ATOM 1072 CA ILE A 201 52.252 16.355 20.080 1.00 18.93 A ATOM 1073 CB ILE A 201 51.784 15.414 18.955 1.00 19.70 A ATOM 1074 CC2 ILE A 201 51.414 16.226 17.716 1.00 20.12 A ATOM 1075 CC1 ILE A 201 52.880 14.395 18.636 1.00 20.03 A ATOM 1076 CD1 ILE A 201 52.408 13.258 17.745 1.00 22.75 A ATOM 1077 C ILE A 201 51.193 17.425 20.270 1.00 19.87 A ATOM 1078 O ILE A 201 50.121 17.161 20.817 1.00 20.08 A ATOM 1079 N ILE A 202 51.508 18.633 19.815 1.00 19.94 A ATOM 1080 CA ILE A 202 50.601 19.772 19.891 1.00 20.45 A ATOM 1081 CB ILE A 202 51.352 21.040 20.356 1.00 22.21 A ATOM 1082 CC2 ILE A 202 50.381 22.220 20.470 1.00 22.67 A ATOM 1083 CC1 ILE A 202 52.033 20.775 21.700 1.00 24.19 A ATOM 1084 CD1 ILE A 202 52.914 21.920 22.169 1.00 25.39 A ATOM 1085 C ILE A 202 50.105 19.999 18.464 1.00 20.71 A ATOM 1086 O ILE A 202 50.910 20.067 17.538 1.00 19.48 A ATOM 1087 N HIS A 203 48.795 20.108 18.270 1.00 18.65 A ATOM 1088 CA HIS A 203 48.280 20.319 16.919 1.00 18.02 A ATOM 1089 CB HIS A 203 46.775 20.057 16.874 1.00 16.31 A ATOM 1090 CC HIS A 203 46.199 20.136 15.495 1.00 18.36 A ATOM 1091 CD2 HIS A 203 46.043 21.186 14.655 1.00 16.42 A ATOM 1092 ND1 HIS A 203 45.759 19.026 14.806 1.00 19.50 A ATOM 1093 CE1 HIS A 203 45.359 19.389 13.600 1.00 17.64 A ATOM 1094 NE2 HIS A 203 45.522 20.694 13.483 1.00 20.87 A ATOM 1095 C HIS A 203 48.589 21.738 16.405 1.00 18.92 A ATOM 1096 O HIS A 203 49.073 21.906 15.282 1.00 16.21 A ATOM 1097 N ARC A 204 48.301 22.744 17.232 1.00 18.60 A ATOM 1098 CA ARC A 204 48.552 24.157 16.914 1.00 19.81 A ATOM 1099 CB ARC A 204 49.998 24.365 16.458 1.00 21.61 A ATOM 1100 CC ARC A 204 51.024 24.137 17.550 1.00 23.82 A ATOM 1101 CD ARC A 204 52.323 24.870 17.252 1.00 27.62 A ATOM 1102 NE ARC A 204 52.932 24.449 15.994 1.00 29.43 A ATOM 1103 CZ ARC A 204 54.125 24.861 15.572 1.00 33.10 A ATOM 1104 NH1 ARC A 204 54.835 25.706 16.311 1.00 32.12 A ATOM 1105 NH2 ARC A 204 54.614 24.426 14.418 1.00 30.25 A ATOM 1106 C ARC A 204 47.624 24.830 15.905 1.00 20.03 A ATOM 1107 O ARC A 204 47.711 26.038 15.698 1.00 20.88 A ATOM 1108 N ASP A 205 46.755 24.071 15.255 1.00 18.96 A ATOM 1109 CA ASP A 205 45.828 24.692 14.325 1.00 17.90 A ATOM 1110 CB ASP A 205 46.418 24.741 12.914 1.00 18.95 A ATOM 1111 CC ASP A 205 45.655 25.688 12.008 1.00 20.36 A ATOM 1112 OD1 ASP A 205 44.939 26.560 12.545 1.00 20.35 A ATOM 1113 OD2 ASP A 205 45.772 25.573 10.771 1.00 22.49 A ATOM 1114 C ASP A 205 44.500 23.956 14.328 1.00 19.60 A ATOM 1115 O ASP A 205 43.876 23.751 13.287 1.00 21.53 A ATOM 1116 N LEU A 206 44.063 23.569 15.521 1.00 18.53 A ATOM 1117 CA LEU A 206 42.813 22.851 15.667 1.00 19.18 A ATOM 1118 CB LEU A 206 42.693 22.295 17.087 1.00 18.94 A ATOM 1119 CC LEU A 206 41.511 21.358 17.346 1.00 23.10 A ATOM 1120 CD1 LEU A 206 41.615 20.142 16.436 1.00 23.01 A ATOM 1121 CD2 LEU A 206 41.504 20.933 18.808 1.00 22.97 A ATOM 1122 C LEU A 206 41.639 23.772 15.361 1.00 19.05 A ATOM 1123 O LEU A 206 41.556 24.880 15.886 1.00 19.25 A ATOM 1124 N LYS A 207 40.740 23.307 14.500 1.00 17.54 A ATOM 1125 CA LYS A 207 39.564 24.081 14.110 1.00 18.60 A ATOM 1126 CB LYS A 207 39.980 25.248 13.196 1.00 18.98 A ATOM 1127 CC LYS A 207 40.786 24.817 11.982 1.00 18.20 A ATOM 1128 CD LYS A 207 41.246 26.000 11.139 1.00 21.42 A ATOM 1129 CE LYS A 207 42.223 25.537 10.062 1.00 23.21 A ATOM 1130 NZ LYS A 207 42.561 26.604 9.084 1.00 29.61 A ATOM 1131 C LYS A 207 38.566 23.181 13.388 1.00 18.18 A ATOM 1132 O LYS A 207 38.921 22.100 12.915 1.00 18.11 A ATOM 1133 N PRO A 208 37.298 23.614 13.293 1.00 20.26 A ATOM 1134 CD PRO A 208 36.713 24.833 13.882 1.00 18.79 A ATOM 1135 CA PRO A 208 36.272 22.814 12.616 1.00 19.67 A ATOM 1136 CB PRO A 208 35.063 23.742 12.608 1.00 19.45 A ATOM 1137 CG PRO A 208 35.231 24.509 13.891 1.00 21.81 A ATOM 1138 C PRO A 208 36.674 22.372 11.209 1.00 21.04 A ATOM 1139 O PRO A 208 36.264 21.307 10.751 1.00 21.19 A ATOM 1140 N GLU A 209 37.474 23.188 10.528 1.00 21.69 A ATOM 1141 CA GLU A 209 37.928 22.872 9.170 1.00 22.64 A ATOM 1142 CB GLU 209 38.644 24.084 8.558 0.50 23.65 AC1 ATOM 1143 CG GLU 209 39.253 23.825 7.185 0.50 27.24 AC1 ATOM 1144 CD GLU 209 40.155 24.958 6.716 0.50 29.40 AC1 ATOM 1145 OE1 GLU 209 39.660 26.094 6.553 0.50 29.68 AC1 ATOM 1146 OE2 GLU 209 41.363 24.711 6.511 0.50 30.07 AC1 ATOM 1147 C GLU A 209 38.879 21.668 9.159 1.00 22.28 A ATOM 1148 O GLU A 209 38.955 20.933 8.170 1.00 21.36 A ATOM 1149 N ASN A 210 39.600 21.490 10.263 1.00 19.90 A ATOM 1150 CA ASN A 210 40.574 20.412 10.436 1.00 19.44 A ATOM 1151 CB ASN A 210 41.744 20.912 11.287 1.00 20.07 A ATOM 1152 CG ASN A 210 42.746 21.698 10.479 1.00 25.77 A ATOM 1153 OD1 ASN A 210 43.571 22.427 11.029 1.00 26.73 A ATOM 1154 ND2 ASN A 210 42.687 21.548 9.158 1.00 25.15 A ATOM 1155 C ASN A 210 40.005 19.151 11.078 1.00 18.63 A ATOM 1156 O ASN A 210 40.712 18.154 11.234 1.00 18.29 A ATOM 1157 N ILE A 211 38.739 19.202 11.469 1.00 16.31 A ATOM 1158 CA ILE A 211 38.090 18.058 12.085 1.00 15.49 A ATOM 1159 CB ILE A 211 37.336 18.488 13.354 1.00 15.40 A ATOM 1160 CG2 ILE A 211 36.582 17.311 13.950 1.00 14.59 A ATOM 1161 CG1 ILE A 211 38.342 19.046 14.365 1.00 15.91 A ATOM 1162 CD1 ILE A 211 37.720 19.669 15.590 1.00 15.98 A ATOM 1163 C ILE A 211 37.131 17.485 11.059 1.00 17.26 A ATOM 1164 O ILE A 211 35.995 17.947 10.926 1.00 18.16 A ATOM 1165 N LEU 212 37.599 16.486 10.317 1.00 15.97 A ATOM 1166 CA LEU A 212 36.784 15.875 9.274 1.00 17.08 A ATOM 1167 CB LEU A 212 37.685 15.249 8.202 1.00 17.78 A ATOM 1168 CG LEU A 212 38.785 16.157 7.640 1.00 18.92 A ATOM 1169 CD1 LEU A 212 39.476 15.450 6.485 1.00 22.09 A ATOM 1170 CD2 LEU A 212 38.188 17.482 7.166 1.00 19.91 A ATOM 1171 C LEU A 212 35.843 14.825 9.837 1.00 18.35 A ATOM 1172 O LEU A 212 35.957 14.433 11.002 1.00 19.39 A ATOM 1173 N LEU A 213 34.915 14.368 9.000 1.00 17.84 A ATOM 1174 CA LEU A 213 33.942 13.362 9.403 1.00 19.94 A ATOM 1175 CB LEU A 213 32.556 14.004 9.487 1.00 20.84 A ATOM 1176 CG LEU A 213 32.396 15.059 10.583 1.00 20.31 A ATOM 1177 CD1 LEU A 213 31.124 15.837 10.367 1.00 22.75 A ATOM 1178 CD2 LEU A 213 32.379 14.378 11.940 1.00 23.93 A ATOM 1179 C LEU A 213 33.914 12.187 8.426 1.00 20.98 A ATOM 1180 O LEU A 213 33.743 12.379 7.218 1.00 19.55 A ATOM 1181 N ASN A 214 34.088 10.970 8.935 1.00 20.44 A ATOM 1182 CA ASN A 214 34.055 9.814 8.049 1.00 23.77 A ATOM 1183 CB ASN A 214 34.745 8.596 8.674 1.00 25.30 A ATOM 1184 CG ASN A 214 34.077 8.127 9.948 1.00 32.04 A ATOM 1185 OD1 ASN A 214 32.908 8.422 10.206 1.00 34.43 A ATOM 1186 ND2 ASN A 214 34.818 7.369 10.752 1.00 33.85 A ATOM 1187 C ASN A 214 32.618 9.466 7.693 1.00 24.07 A ATOM 1188 O ASN A 214 31.672 10.113 8.150 1.00 19.94 A ATOM 1189 N GLU A 215 32.459 8.433 6.879 1.00 25.77 A ATOM 1190 CA GLU A 215 31.138 8.003 6.445 1.00 28.69 A ATOM 1191 CB GLU A 215 31.275 6.796 5.513 1.00 31.98 A ATOM 1192 CG GLU A 215 29.970 6.334 4.896 1.00 40.22 A ATOM 1193 CD GLU A 215 30.182 5.312 3.795 1.00 44.27 A ATOM 1194 OE1 GLU A 215 30.817 4.268 4.065 1.00 46.46 A ATOM 1195 OE2 GLU A 215 29.716 5.556 2.660 1.00 46.13 A ATOM 1196 C GLU A 215 30.188 7.673 7.601 1.00 28.41 A ATOM 1197 O GLU A 215 28.971 7.769 7.447 1.00 28.52 A ATOM 1198 N ASP A 216 30.737 7.287 8.752 1.00 26.77 A ATOM 1199 CA ASP A 216 29.914 6.953 9.917 1.00 27.28 A ATOM 1200 CB ASP A 216 30.538 5.795 10.696 1.00 31.27 A ATOM 1201 CC ASP A 216 30.390 4.466 9.979 1.00 37.61 A ATOM 1202 OD1 ASP A 216 29.274 4.170 9.499 1.00 39.45 A ATOM 1203 OD2 ASP A 216 31.382 3.710 9.902 1.00 41.84 A ATOM 1204 C ASP A 216 29.697 8.135 10.862 1.00 26.37 A ATOM 1205 O ASP A 216 29.136 7.984 11.950 1.00 25.73 A ATOM 1206 N MET A 217 30.156 9.306 10.441 1.00 23.02 A ATOM 1207 CA MET A 217 30.015 10.527 11.218 1.00 21.83 A ATOM 1208 CB MET A 217 28.537 10.789 11.517 1.00 23.24 A ATOM 1209 CC MET A 217 27.742 11.186 10.274 1.00 22.98 A ATOM 1210 SD MET A 217 28.464 12.616 9.430 1.00 27.57 A ATOM 1211 CE MET A 217 27.679 13.974 10.332 1.00 26.68 A ATOM 1212 C MET A 217 30.844 10.618 12.502 1.00 21.51 A ATOM 1213 O MET A 217 30.474 11.323 13.440 1.00 18.62 A ATOM 1214 N HIS A 218 31.957 9.892 12.544 1.00 20.10 A ATOM 1215 CA HIS A 218 32.873 9.964 13.678 1.00 19.86 A ATOM 1216 CB HIS A 218 33.482 8.594 13.977 1.00 20.21 A ATOM 1217 CC HIS A 218 32.551 7.667 14.698 1.00 22.40 A ATOM 1218 CD2 HIS A 218 31.910 6.547 14.287 1.00 21.27 A ATOM 1219 ND1 HIS A 218 32.177 7.863 16.011 1.00 19.59 A ATOM 1220 CE1 HIS A 218 31.348 6.902 16.379 1.00 21.88 A ATOM 1221 NE2 HIS A 218 31.168 6.091 15.351 1.00 22.08 A ATOM 1222 C HIS A 218 33.947 10.921 13.172 1.00 19.10 A ATOM 1223 O HIS A 218 34.170 11.004 11.965 1.00 20.31 A ATOM 1224 N ILE A 219 34.617 11.638 14.067 1.00 17.21 A ATOM 1225 CA ILE A 219 35.628 12.586 13.618 1.00 15.26 A ATOM 1226 CB ILE A 219 35.987 13.614 14.716 1.00 15.38 A ATOM 1227 CC2 ILE A 219 34.722 14.305 15.221 1.00 14.58 A ATOM 1228 CC1 ILE A 219 36.734 12.919 15.864 1.00 14.46 A ATOM 1229 CD1 ILE A 219 37.279 13.885 16.911 1.00 13.74 A ATOM 1230 C ILE A 219 36.929 11.944 13.161 1.00 16.21 A ATOM 1231 O ILE A 219 37.238 10.799 13.500 1.00 15.88 A ATOM 1232 N GIN A 220 37.677 12.711 12.378 1.00 15.62 A ATOM 1233 CA GIN A 220 38.980 12.316 11.876 1.00 17.84 A ATOM 1234 CB GIN A 220 38.872 11.595 10.525 1.00 20.00 A ATOM 1235 CC CLN A 220 38.463 10.129 10.659 1.00 26.97 A ATOM 1236 CD CLN A 220 38.648 9.343 9.372 1.00 29.95 A ATOM 1237 OE1 CLN A 220 37.968 9.590 8.373 1.00 33.12 A ATOM 1238 NE2 CLN A 220 39.578 8.393 9.389 1.00 30.47 A ATOM 1239 C CLN A 220 39.757 13.610 11.735 1.00 17.00 A ATOM 1240 O CLN A 220 39.609 14.339 10.751 1.00 18.27 A ATOM 1241 N ILE A 221 40.566 13.906 12.746 1.00 14.34 A ATOM 1242 CA ILE A 221 41.361 15.120 12.753 1.00 14.46 A ATOM 1243 CB ILE A 221 41.867 15.416 14.175 1.00 12.30 A ATOM 1244 CC2 ILE A 221 42.764 16.656 14.167 1.00 14.78 A ATOM 1245 Cd ILE A 221 40.660 15.613 15.102 1.00 13.92 A ATOM 1246 CD1 ILE A 221 41.003 15.901 16.543 1.00 15.06 A ATOM 1247 C ILE A 221 42.536 14.996 11.783 1.00 15.44 A ATOM 1248 O ILE A 221 43.106 13.915 11.613 1.00 13.93 A ATOM 1249 N THR A 222 42.877 16.101 11.127 1.00 15.36 A ATOM 1250 CA THR A 222 43.980 16.098 10.174 1.00 17.52 A ATOM 1251 CB THR A 222 43.470 15.836 8.750 1.00 19.92 A ATOM 1252 OG1 THR A 222 44.587 15.637 7.875 1.00 18.78 A ATOM 1253 CG2 THR A 222 42.630 17.018 8.257 1.00 18.16 A ATOM 1254 C THR A 222 44.735 17.428 10.192 1.00 19.60 A ATOM 1255 O THR A 222 44.509 18.257 11.084 1.00 18.59 A ATOM 1256 N ASP A 223 45.630 17.610 9.216 1.00 18.69 A ATOM 1257 CA ASP A 223 46.440 18.825 9.069 1.00 20.12 A ATOM 1258 CB ASP A 223 45.532 20.065 9.108 1.00 23.51 A ATOM 1259 CG ASP A 223 46.248 21.335 8.670 1.00 27.09 A ATOM 1260 OD1 ASP A 223 47.283 21.227 7.975 1.00 26.28 A ATOM 1261 OD2 ASP A 223 45.765 22.438 9.009 1.00 26.15 A ATOM 1262 C ASP A 223 47.516 18.913 10.150 1.00 21.73 A ATOM 1263 O ASP A 223 47.439 19.751 11.055 1.00 22.76 A ATOM 1264 N PHE A 224 48.535 18.063 10.027 1.00 20.75 A ATOM 1265 CA PHE A 224 49.611 17.988 11.009 1.00 20.11 A ATOM 1266 CB PHE A 224 49.805 16.527 11.424 1.00 20.62 A ATOM 1267 CG PHE A 224 48.682 15.991 12.263 1.00 21.41 A ATOM 1268 CD1 PHE A 224 48.598 16.312 13.614 1.00 23.05 A ATOM 1269 CD2 PHE A 224 47.681 15.212 11.693 1.00 22.27 A ATOM 1270 CE1 PHE A 224 47.528 15.868 14.389 1.00 23.30 A ATOM 1271 CE2 PHE A 224 46.606 14.763 12.457 1.00 21.11 A ATOM 1272 CZ PHE A 224 46.530 15.093 13.807 1.00 22.02 A ATOM 1273 C PHE A 224 50.957 18.583 10.619 1.00 20.45 A ATOM 1274 O PHE A 224 51.905 18.547 11.407 1.00 20.73 A ATOM 1275 N GLY A 225 51.049 19.125 9.412 1.00 22.02 A ATOM 1276 CA GLY A 225 52.301 19.713 8.981 1.00 22.66 A ATOM 1277 C GLY A 225 52.742 20.822 9.920 1.00 24.99 A ATOM 1278 O GLY A 225 53.939 21.041 10.122 1.00 24.52 A ATOM 1279 N THR A 226 51.779 21.524 10.508 1.00 23.50 A ATOM 1280 CA THR A 226 52.106 22.613 11.416 1.00 25.16 A ATOM 1281 CB THR A 226 51.199 23.829 11.160 1.00 24.76 A ATOM 1282 OG1 THR A 226 49.831 23.410 11.113 1.00 22.68 A ATOM 1283 CG2 THR A 226 51.571 24.490 9.834 1.00 25.00 A ATOM 1284 C THR A 226 52.046 22.233 12.894 1.00 25.79 A ATOM 1285 O THR A 226 52.019 23.100 13.768 1.00 24.54 A ATOM 1286 N ALA A 227 52.037 20.935 13.173 1.00 24.97 A ATOM 1287 CA ALA A 227 52.004 20.475 14.550 1.00 25.49 A ATOM 1288 CB ALA A 227 51.659 18.993 14.607 1.00 22.85 A ATOM 1289 C ALA A 227 53.384 20.715 15.149 1.00 27.70 A ATOM 1290 O ALA A 227 54.331 21.047 14.435 1.00 26.60 A ATOM 1291 N LYS A 228 53.491 20.558 16.461 1.00 28.53 A ATOM 1292 CA LYS A 228 54.760 20.745 17.149 1.00 32.12 A ATOM 1293 CB LYS A 228 54.699 21.974 18.054 1.00 33.81 A ATOM 1294 CG LYS A 228 56.007 22.294 18.765 1.00 41.23 A ATOM 1295 CD LYS A 228 57.082 22.725 17.768 1.00 47.57 A ATOM 1296 CE LYS A 228 58.401 23.056 18.462 1.00 49.82 A ATOM 1297 NZ LYS A 228 59.459 23.425 17.480 1.00 51.49 A ATOM 1298 C LYS A 228 55.019 19.504 17.985 1.00 33.25 A ATOM 1299 O LYS A 228 54.190 19.129 18.815 1.00 33.70 A ATOM 1300 N VAL A 229 56.159 18.860 17.756 1.00 33.64 A ATOM 1301 CA VAL A 229 56.516 17.661 18.501 1.00 34.66 A ATOM 1302 CB VAL A 229 57.248 16.646 17.609 1.00 33.50 A ATOM 1303 CG1 VAL A 229 57.619 15.419 18.415 1.00 32.34 A ATOM 1304 CG2 VAL A 229 56.370 16.264 16.436 1.00 34.25 A ATOM 1305 C VAL A 229 57.420 18.035 19.668 1.00 37.57 A ATOM 1306 O VAL A 229 58.581 18.392 19.474 1.00 35.91 A ATOM 1307 N LEU A 230 56.877 17.948 20.878 1.00 40.57 A ATOM 1308 CA LEU A 230 57.615 18.289 22.088 1.00 46.10 A ATOM 1309 CB LEU A 230 56.654 18.417 23.270 1.00 44.71 A ATOM 1310 CG LEU A 230 55.627 19.545 23.207 1.00 44.50 A ATOM 1311 CD1 LEU A 230 54.673 19.430 24.383 1.00 44.39 A ATOM 1312 CD2 LEU A 230 56.340 20.885 23.214 1.00 44.81 A ATOM 1313 C LEU A 230 58.695 17.279 22.440 1.00 50.42 A ATOM 1314 O LEU A 230 58.603 16.104 22.089 1.00 51.64 A ATOM 1315 N SER A 231 59.717 17.756 23.145 1.00 55.81 A ATOM 1316 CA SER A 231 60.824 16.914 23.583 1.00 61.14 A ATOM 1317 CB SER A 231 62.077 17.200 22.750 1.00 61.27 A ATOM 1318 OG SER A 231 62.444 18.568 22.823 1.00 62.85 A ATOM 1319 C SER A 231 61.124 17.126 25.071 1.00 64.65 A ATOM 1320 O SER A 231 61.392 16.164 25.794 1.00 65.70 A ATOM 1321 N PRO A 232 61.081 18.387 25.549 1.00 67.54 A ATOM 1322 CD PRO A 232 60.854 19.651 24.823 1.00 68.60 A ATOM 1323 CA PRO A 232 61.358 18.655 26.966 1.00 68.74 A ATOM 1324 CB PRO A 232 61.109 20.158 27.086 1.00 68.83 A ATOM 1325 CG PRO A 232 61.505 20.666 25.737 1.00 68.96 A ATOM 1326 C PRO A 232 60.460 17.846 27.899 1.00 69.17 A ATOM 1327 O PRO A 232 59.335 17.494 27.541 1.00 69.94 A ATOM 1328 N ALA A 237 57.424 23.198 27.637 1.00 80.06 A ATOM 1329 CA ALA A 237 56.783 23.047 26.335 1.00 79.29 A ATOM 1330 CB ALA A 237 55.275 22.907 26.512 1.00 78.64 A ATOM 1331 C ALA A 237 57.092 24.239 25.433 1.00 79.07 A ATOM 1332 O ALA A 237 56.250 25.113 25.249 1.00 79.47 A ATOM 1333 N ALA A 238 58.297 24.280 24.871 1.00 78.57 A ATOM 1334 CA ALA A 238 58.683 25.383 23.992 1.00 78.50 A ATOM 1335 CB ALA A 238 60.186 25.347 23.728 1.00 78.50 A ATOM 1336 C ALA A 238 57.920 25.327 22.673 1.00 78.15 A ATOM 1337 O ALA A 238 57.243 24.341 22.375 1.00 77.96 A ATOM 1338 N ALA A 239 58.027 26.393 21.887 1.00 77.28 A ATOM 1339 CA ALA A 239 57.338 26.452 20.603 1.00 76.27 A ATOM 1340 CB ALA A 239 55.849 26.489 20.827 1.00 76.61 A ATOM 1341 C ALA A 239 57.766 27.667 19.793 1.00 75.38 A ATOM 1342 O ALA A 239 58.955 27.955 19.700 1.00 75.89 A ATOM 1343 N ASN A 240 56.781 28.357 19.214 1.00 73.95 A ATOM 1344 CA ASN A 240 56.967 29.553 18.389 1.00 71.07 A ATOM 1345 CB ASN A 240 58.151 30.400 18.874 1.00 71.47 A ATOM 1346 CG ASN A 240 59.459 30.055 18.174 1.00 72.06 A ATOM 1347 OD1 ASN A 240 59.575 30.149 16.943 1.00 72.03 A ATOM 1348 ND2 ASN A 240 60.470 29.665 18.964 1.00 71.91 A ATOM 1349 C ASN A 240 57.188 29.178 16.928 1.00 69.41 A ATOM 1350 O ASN A 240 57.480 28.024 16.624 1.00 70.09 A ATOM 1351 N ALA A 241 57.055 30.165 16.038 1.00 66.62 A ATOM 1352 CA ALA A 241 57.246 30.013 14.585 1.00 63.94 A ATOM 1353 C ALA A 241 55.952 30.080 13.772 1.00 60.63 A ATOM 1354 O ALA A 241 55.840 30.880 12.845 1.00 61.29 A ATOM 1355 CB ALA A 241 57.979 28.704 14.246 1.00 65.23 A ATOM 1356 N PHE A 242 54.984 29.236 14.113 1.00 56.72 A ATOM 1357 CA PHE A 242 53.712 29.196 13.394 1.00 52.53 A ATOM 1358 CB PHE A 242 53.419 27.767 12.923 1.00 49.14 A ATOM 1359 CG PHE A 242 52.040 27.590 12.354 1.00 47.38 A ATOM 1360 CD1 PHE A 242 51.731 28.067 11.085 1.00 47.69 A ATOM 1361 CD2 PHE A 242 51.038 26.975 13.102 1.00 45.45 A ATOM 1362 CE1 PHE A 242 50.445 27.937 10.565 1.00 46.75 A ATOM 1363 CE2 PHE A 242 49.751 26.840 12.594 1.00 45.41 A ATOM 1364 CZ PHE A 242 49.453 27.323 11.322 1.00 46.55 A ATOM 1365 C PHE A 242 52.534 29.688 14.229 1.00 50.08 A ATOM 1366 O PHE A 242 52.502 29.505 15.444 1.00 49.86 A ATOM 1367 N VAL A 243 51.566 30.305 13.557 1.00 47.67 A ATOM 1368 CA VAL A 243 50.355 30.809 14.200 1.00 46.21 A ATOM 1369 CB VAL A 243 50.340 32.352 14.258 1.00 47.36 A ATOM 1370 CG1 VAL A 243 49.012 32.844 14.825 1.00 47.54 A ATOM 1371 CG2 VAL A 243 51.497 32.842 15.109 1.00 48.50 A ATOM 1372 C VAL A 243 49.150 30.342 13.389 1.00 44.12 A ATOM 1373 O VAL A 243 48.956 30.765 12.247 1.00 44.46 A ATOM 1374 N GLY A 244 48.348 29.467 13.985 1.00 40.48 A ATOM 1375 CA GLY A 244 47.176 28.941 13.306 1.00 37.65 A ATOM 1376 C GLY A 244 46.101 29.960 12.964 1.00 35.39 A ATOM 1377 O GLY A 244 46.313 31.168 13.065 1.00 35.92 A ATOM 1378 N THR A 245 44.936 29.463 12.560 1.00 33.30 A ATOM 1379 CA THR A 245 43.813 30.312 12.184 1.00 30.20 A ATOM 1380 CB THR A 245 42.593 29.450 11.829 1.00 32.00 A ATOM 1381 OG1 THR A 245 42.952 28.573 10.755 1.00 32.81 A ATOM 1382 CG2 THR A 245 41.419 30.319 11.390 1.00 28.34 A ATOM 1383 C THR A 245 43.476 31.296 13.296 1.00 27.96 A ATOM 1384 O THR A 245 43.212 30.907 14.434 1.00 25.46 A ATOM 1385 N ALA A 246 43.486 32.576 12.938 1.00 25.22 A ATOM 1386 CA ALA A 246 43.247 33.675 13.867 1.00 23.27 A ATOM 1387 CB ALA A 246 42.956 34.955 13.082 1.00 22.94 A ATOM 1388 C ALA A 246 42.178 33.475 14.934 1.00 21.27 A ATOM 1389 O ALA A 246 42.431 33.705 16.114 1.00 20.93 A ATOM 1390 N GLN A 247 40.988 33.047 14.536 1.00 19.67 A ATOM 1391 CA GLN A 247 39.911 32.886 15.504 1.00 20.17 A ATOM 1392 CB GLN 247 38.608 32.535 14.779 0.50 21.89 AC1 ATOM 1393 CG GLN 247 38.522 33.076 13.355 0.50 26.18 AC1 ATOM 1394 CD GLN 247 37.220 33.794 13.064 0.50 27.30 AC1 ATOM 1395 OE1 GLN 247 36.172 33.447 13.605 0.50 30.13 AC1 ATOM 1396 NE2 GLN 247 37.278 34.792 12.189 0.50 28.70 AC1 ATOM 1397 C GLN A 247 40.181 31.849 16.595 1.00 19.43 A ATOM 1398 O GLN A 247 39.546 31.883 17.648 1.00 18.93 A ATOM 1399 N TYR A 248 41.132 30.948 16.359 1.00 18.60 A ATOM 1400 CA TYR A 248 41.441 29.896 17.329 1.00 19.20 A ATOM 1401 CB TYR A 248 41.333 28.529 16.642 1.00 17.53 A ATOM 1402 CG TYR A 248 40.013 28.362 15.927 1.00 19.32 A ATOM 1403 CD1 TYR A 248 38.859 28.010 16.625 1.00 17.69 A ATOM 1404 CEl TYR A 248 37.617 27.976 15.990 1.00 18.18 A ATOM 1405 CD2 TYR A 248 39.897 28.664 14.569 1.00 16.87 A ATOM 1406 CE2 TYR A 248 38.665 28.635 13.924 1.00 19.17 A ATOM 1407 CZ TYR A 248 37.527 28.295 14.643 1.00 19.46 A ATOM 1408 OH TYR A 248 36.299 28.311 14.023 1.00 18.98 A ATOM 1409 C TYR A 248 42.810 30.039 17.993 1.00 20.42 A ATOM 1410 O TYR A 248 43.208 29.191 18.792 1.00 19.19 A ATOM 1411 N VAL A 249 43.523 31.114 17.673 1.00 20.20 A ATOM 1412 CA VAL A 249 44.841 31.343 18.251 1.00 20.91 A ATOM 1413 CB VAL A 249 45.542 32.532 17.570 1.00 21.18 A ATOM 1414 CG1 VAL A 249 46.821 32.896 18.317 1.00 22.45 A ATOM 1415 CG2 VAL A 249 45.862 32.170 16.139 1.00 24.01 A ATOM 1416 C VAL A 249 44.764 31.606 19.750 1.00 21.52 A ATOM 1417 O VAL A 249 43.915 32.368 20.216 1.00 22.72 A ATOM 1418 N SER A 250 45.654 30.965 20.503 1.00 20.70 A ATOM 1419 CA SER A 250 45.697 31.133 21.951 1.00 21.65 A ATOM 1420 CB SER A 250 46.370 29.919 22.613 1.00 22.02 A ATOM 1421 OG SER A 250 47.692 29.725 22.132 1.00 22.12 A ATOM 1422 C SER A 250 46.476 32.402 22.280 1.00 22.13 A ATOM 1423 O SER A 250 47.332 32.828 21.511 1.00 22.77 A ATOM 1424 N PRO A 251 46.180 33.029 23.425 1.00 22.23 A ATOM 1425 CD PRO A 251 45.163 32.684 24.433 1.00 22.97 A ATOM 1426 CA PRO A 251 46.893 34.254 23.800 1.00 22.52 A ATOM 1427 CB PRO A 251 46.233 34.650 25.127 1.00 23.06 A ATOM 1428 CG PRO A 251 45.726 33.329 25.676 1.00 22.55 A ATOM 1429 C PRO A 251 48.414 34.115 23.907 1.00 22.15 A ATOM 1430 O PRO A 251 49.143 35.047 23.563 1.00 22.62 A ATOM 1431 N GLU A 252 48.901 32.966 24.367 1.00 20.69 A ATOM 1432 CA GLU A 252 50.347 32.772 24.500 1.00 21.40 A ATOM 1433 CB GLU A 252 50.673 31.382 25.071 1.00 20.59 A ATOM 1434 CC GLU A 252 49.993 30.232 24.352 1.00 21.91 A ATOM 1435 CD GLU A 252 48.691 29.822 25.014 1.00 21.51 A ATOM 1436 OE1 GLU A 252 47.989 30.707 25.550 1.00 21.46 A ATOM 1437 0E2 GLU A 252 48.367 28.613 24.993 1.00 20.23 A ATOM 1438 C GLU A 252 51.071 32.970 23.167 1.00 22.99 A ATOM 1439 O GLU A 252 52.191 33.480 23.136 1.00 23.17 A ATOM 1440 N LEU A 253 50.441 32.576 22.064 1.00 23.00 A ATOM 1441 CA LEU A 253 51.068 32.753 20.758 1.00 25.62 A ATOM 1442 CB LEU A 253 50.277 32.029 19.669 1.00 26.75 A ATOM 1443 CC LEU A 253 50.743 30.620 19.296 1.00 31.87 A ATOM 1444 CD1 LEU A 253 50.433 29.651 20.422 1.00 31.81 A ATOM 1445 CD2 LEU A 253 50.044 30.179 18.015 1.00 31.86 A ATOM 1446 C LEU A 253 51.201 34.228 20.371 1.00 26.94 A ATOM 1447 O LEU A 253 52.107 34.601 19.626 1.00 27.09 A ATOM 1448 N LEU A 254 50.297 35.059 20.877 1.00 25.83 A ATOM 1449 CA LEU A 254 50.297 36.485 20.564 1.00 27.26 A ATOM 1450 CB LEU A 254 48.858 37.006 20.564 1.00 25.84 A ATOM 1451 CC LEU A 254 47.882 36.290 19.621 1.00 24.69 A ATOM 1452 CD1 LEU A 254 46.459 36.724 19.932 1.00 23.64 A ATOM 1453 CD2 LEU A 254 48.236 36.597 18.177 1.00 24.24 A ATOM 1454 C LEU A 254 51.134 37.314 21.537 1.00 30.62 A ATOM 1455 O LEU A 254 51.633 38.383 21.187 1.00 32.35 A ATOM 1456 N THR A 255 51.292 36.821 22.758 1.00 32.47 A ATOM 1457 CA THR A 255 52.056 37.547 23.759 1.00 36.70 A ATOM 1458 CB THR A 255 51.368 37.478 25.127 1.00 34.51 A ATOM 1459 OG1 THR A 255 51.188 36.106 25.494 1.00 35.49 A ATOM 1460 CC2 THR A 255 50.013 38.166 25.077 1.00 33.40 A ATOM 1461 C THR A 255 53.477 37.035 23.910 1.00 40.09 A ATOM 1462 O THR A 255 54.430 37.793 23.772 1.00 43.69 A ATOM 1463 N CLU A 256 53.617 35.747 24.189 1.00 44.77 A ATOM 1464 CA CLU A 256 54.932 35.144 24.382 1.00 49.15 A ATOM 1465 CB CLU A 256 54.866 34.143 25.534 1.00 51.24 A ATOM 1466 CC CLU A 256 54.514 34.786 26.862 1.00 56.03 A ATOM 1467 CD CLU A 256 54.053 33.780 27.893 1.00 58.83 A ATOM 1468 OE1 CLU A 256 54.766 32.776 28.107 1.00 62.13 A ATOM 1469 OE2 CLU A 256 52.979 33.996 28.494 1.00 60.34 A ATOM 1470 C CLU A 256 55.475 34.456 23.137 1.00 50.09 A ATOM 1471 O CLU A 256 56.616 33.995 23.127 1.00 50.42 A ATOM 1472 N LYS A 257 54.658 34.389 22.090 1.00 51.21 A ATOM 1473 CA LYS A 257 55.064 33.746 20.845 1.00 51.22 A ATOM 1474 CB LYS A 257 56.244 34.502 20.227 1.00 53.28 A ATOM 1475 CC LYS A 257 56.558 34.125 18.790 1.00 55.19 A ATOM 1476 CD LYS A 257 57.709 34.961 18.253 1.00 57.52 A ATOM 1477 CE LYS A 257 57.952 34.694 16.777 1.00 58.52 A ATOM 1478 NZ LYS A 257 58.290 33.268 16.515 1.00 60.88 A ATOM 1479 C LYS A 257 55.467 32.302 21.138 1.00 50.74 A ATOM 1480 O LYS A 257 56.432 31.790 20.577 1.00 52.26 A ATOM 1481 N SER A 258 54.721 31.654 22.027 1.00 48.07 A ATOM 1482 CA SER A 258 54.999 30.273 22.402 1.00 46.87 A ATOM 1483 CB SER A 258 55.590 30.229 23.812 1.00 48.88 A ATOM 1484 OG SER A 258 54.741 30.892 24.734 1.00 53.14 A ATOM 1485 C SER A 258 53.735 29.415 22.342 1.00 44.07 A ATOM 1486 O SER A 258 52.617 29.932 22.417 1.00 44.17 A ATOM 1487 N ALA A 259 53.917 28.105 22.204 1.00 38.30 A ATOM 1488 CA ALA A 259 52.793 27.180 22.127 1.00 34.73 A ATOM 1489 CB ALA A 259 52.551 26.779 20.684 1.00 34.16 A ATOM 1490 C ALA A 259 53.042 25.940 22.977 1.00 32.34 A ATOM 1491 O ALA A 259 54.172 25.459 23.086 1.00 31.81 A ATOM 1492 N CYS A 260 51.975 25.428 23.579 1.00 28.58 A ATOM 1493 CA CYS A 260 52.056 24.244 24.425 1.00 26.27 A ATOM 1494 CB CYS A 260 52.183 24.654 25.892 1.00 26.53 A ATOM 1495 SG CYS A 260 50.846 25.739 26.469 1.00 32.91 A ATOM 1496 C CYS A 260 50.786 23.435 24.224 1.00 22.83 A ATOM 1497 O CYS A 260 49.892 23.856 23.495 1.00 22.14 A ATOM 1498 N LYS A 261 50.706 22.277 24.868 1.00 20.02 A ATOM 1499 CA LYS A 261 49.526 21.434 24.744 1.00 20.65 A ATOM 1500 CB LYS A 261 49.619 20.243 25.696 1.00 23.28 A ATOM 1501 CG LYS A 261 50.716 19.253 25.347 1.00 27.44 A ATOM 1502 CD LYS A 261 50.732 18.117 26.350 1.00 29.98 A ATOM 1503 CE LYS A 261 51.922 17.203 26.134 1.00 32.34 A ATOM 1504 NZ LYS A 261 51.940 16.121 27.153 1.00 33.28 A ATOM 1505 C LYS A 261 48.268 22.229 25.062 1.00 19.20 A ATOM 1506 O LYS A 261 47.253 22.092 24.387 1.00 18.08 A ATOM 1507 N SER A 262 48.358 23.068 26.089 1.00 16.92 A ATOM 1508 CA SER A 262 47.235 23.883 26.534 1.00 18.13 A ATOM 1509 CB SER A 262 47.644 24.698 27.770 1.00 18.27 A ATOM 1510 CO SER A 262 46.517 25.258 28.421 1.00 22.53 A ATOM 1511 C SER A 262 46.736 24.811 25.424 1.00 16.77 A ATOM 1512 O SER A 262 45.591 25.254 25.450 1.00 15.69 A ATOM 1513 N SER A 263 47.595 25.118 24.456 1.00 16.44 A ATOM 1514 CA SER A 263 47.175 25.970 23.347 1.00 16.89 A ATOM 1515 CB SER A 263 48.340 26.228 22.382 1.00 18.49 A ATOM 1516 OG SER A 263 49.402 26.909 23.031 1.00 22.10 A ATOM 1517 C SER A 263 46.040 25.257 22.612 1.00 17.79 A ATOM 1518 O SER A 263 45.099 25.898 22.148 1.00 17.57 A ATOM 1519 N ASP A 264 46.119 23.928 22.517 1.00 16.30 A ATOM 1520 CA ASP A 264 45.069 23.166 21.836 1.00 16.72 A ATOM 1521 CB ASP A 264 45.483 21.704 21.620 1.00 15.92 A ATOM 1522 CO ASP A 264 46.544 21.539 20.548 1.00 17.93 A ATOM 1523 OD1 ASP A 264 46.642 22.412 19.661 1.00 16.78 A ATOM 1524 OD2 ASP A 264 47.265 20.515 20.579 1.00 16.64 A ATOM 1525 C ASP A 264 43.773 23.194 22.646 1.00 17.67 A ATOM 1526 O ASP A 264 42.681 23.197 22.076 1.00 18.27 A ATOM 1527 N LEU A 265 43.898 23.205 23.974 1.00 15.49 A ATOM 1528 CA LEU A 265 42.730 23.232 24.849 1.00 14.75 A ATOM 1529 CB LEU A 265 43.147 23.038 26.313 1.00 11.38 A ATOM 1530 CO LEU A 265 43.711 21.641 26.621 1.00 14.04 A ATOM 1531 CD1 LEU A 265 44.249 21.579 28.052 1.00 13.96 A ATOM 1532 CD2 LEU A 265 42.619 20.603 26.416 1.00 11.62 A ATOM 1533 C LEU A 265 41.999 24.557 24.675 1.00 15.13 A ATOM 1534 O LEU A 265 40.777 24.620 24.785 1.00 16.75 A ATOM 1535 N TRP A 266 42.746 25.622 24.405 1.00 16.08 A ATOM 1536 CA TRP A 266 42.118 26.918 24.184 1.00 16.96 A ATOM 1537 CB TRP A 266 43.176 28.015 24.023 1.00 17.28 A ATOM 1538 CO TRP A 266 42.618 29.326 23.521 1.00 20.54 A ATOM 1539 CD2 TRP A 266 42.313 30.490 24.301 1.00 20.07 A ATOM 1540 CE2 TRP A 266 41.782 31.459 23.417 1.00 20.46 A ATOM 1541 CE3 TRP A 266 42.435 30.810 25.660 1.00 20.68 A ATOM 1542 CD1 TRP A 266 42.270 29.631 22.231 1.00 19.53 A ATOM 1543 NE1 TRP A 266 41.769 30.908 22.163 1.00 19.61 A ATOM 1544 CZ2 TRP A 266 41.372 32.727 23.850 1.00 20.90 A ATOM 1545 CZ3 TRP A 266 42.026 32.073 26.091 1.00 19.45 A ATOM 1546 CH2 TRP A 266 41.501 33.015 25.185 1.00 20.71 A ATOM 1547 C TRP A 266 41.284 26.795 22.913 1.00 17.22 A ATOM 1548 O TRP A 266 40.139 27.240 22.863 1.00 18.03 A ATOM 1549 N ALA A 267 41.863 26.181 21.886 1.00 17.50 A ATOM 1550 CA ALA A 267 41.155 25.990 20.626 1.00 16.16 A ATOM 1551 CB ALA A 267 42.050 25.290 19.621 1.00 14.28 A ATOM 1552 C ALA A 267 39.901 25.159 20.891 1.00 16.28 A ATOM 1553 O ALA A 267 38.835 25.436 20.346 1.00 16.46 A ATOM 1554 N LEU A 268 40.031 24.144 21.739 1.00 16.57 A ATOM 1555 CA LEU A 268 38.890 23.299 22.084 1.00 17.03 A ATOM 1556 CB LEU A 268 39.292 22.260 23.139 1.00 15.35 A ATOM 1557 CC LEU A 268 38.158 21.429 23.754 1.00 19.00 A ATOM 1558 CD1 LEU A 268 37.505 20.578 22.678 1.00 16.17 A ATOM 1559 CD2 LEU A 268 38.718 20.537 24.881 1.00 17.49 A ATOM 1560 C LEU A 268 37.766 24.179 22.628 1.00 15.72 A ATOM 1561 O LEU A 268 36.603 24.031 22.247 1.00 15.28 A ATOM 1562 N GLY A 269 38.119 25.099 23.520 1.00 14.34 A ATOM 1563 CA GLY A 269 37.124 25.989 24.092 1.00 13.39 A ATOM 1564 C GLY A 269 36.406 26.808 23.031 1.00 14.94 A ATOM 1565 O GLY A 269 35.193 27.014 23.114 1.00 14.76 A ATOM 1566 N CYS A 270 37.146 27.279 22.030 1.00 13.86 A ATOM 1567 CA CYS A 270 36.539 28.061 20.958 1.00 16.80 A ATOM 1568 CB CYS A 270 37.611 28.634 20.023 1.00 15.97 A ATOM 1569 SQ CYS A 270 38.751 29.810 20.780 1.00 20.48 A ATOM 1570 C CYS A 270 35.598 27.175 20.140 1.00 17.50 A ATOM 1571 O CYS A 270 34.516 27.604 19.741 1.00 18.38 A ATOM 1572 N ILE A 271 36.022 25.939 19.887 1.00 16.99 A ATOM 1573 CA ILE A 271 35.221 25.004 19.104 1.00 16.66 A ATOM 1574 CB ILE A 271 36.038 23.741 18.778 1.00 16.53 A ATOM 1575 CG2 ILE A 271 35.155 22.694 18.102 1.00 16.34 A ATOM 1576 Cd ILE A 271 37.222 24.129 17.882 1.00 15.59 A ATOM 1577 CD1 ILE A 271 38.239 23.018 17.690 1.00 14.88 A ATOM 1578 C ILE A 271 33.920 24.626 19.809 1.00 16.74 A ATOM 1579 O ILE A 271 32.865 24.576 19.179 1.00 17.12 A ATOM 1580 N ILE A 272 33.990 24.357 21.111 1.00 16.13 A ATOM 1581 CA ILE A 272 32.785 24.021 21.862 1.00 18.30 A ATOM 1582 CB ILE A 272 33.097 23.747 23.346 1.00 17.77 A ATOM 1583 CG2 ILE A 272 31.796 23.666 24.152 1.00 17.96 A ATOM 1584 Cd ILE A 272 33.877 22.437 23.481 1.00 19.55 A ATOM 1585 CD1 ILE A 272 34.446 22.217 24.886 1.00 18.64 A ATOM 1586 C ILE A 272 31.824 25.207 21.776 1.00 19.51 A ATOM 1587 O ILE A 272 30.624 25.037 21.554 1.00 20.44 A ATOM 1588 N TYR A 273 32.362 26.409 21.947 1.00 18.52 A ATOM 1589 CA TYR A 273 31.553 27.615 21.881 1.00 20.48 A ATOM 1590 CB TYR A 273 32.418 28.847 22.162 1.00 18.98 A ATOM 1591 Cd TYR A 273 31.663 30.161 22.125 1.00 20.26 A ATOM 1592 CD1 TYR A 273 31.229 30.709 20.916 1.00 20.67 A ATOM 1593 CEl TYR A 273 30.536 31.917 20.880 1.00 20.98 A ATOM 1594 CD2 TYR A 273 31.383 30.857 23.302 1.00 19.82 A ATOM 1595 CE2 TYR A 273 30.691 32.062 23.280 1.00 20.62 A ATOM 1596 CZ TYR A 273 30.271 32.587 22.067 1.00 21.15 A ATOM 1597 OH TYR A 273 29.588 33.776 22.049 1.00 21.86 A ATOM 1598 C TYR A 273 30.902 27.730 20.507 1.00 21.54 A ATOM 1599 O TYR A 273 29.719 28.049 20.401 1.00 22.80 A ATOM 1600 N GLN A 274 31.676 27.454 19.461 1.00 21.05 A ATOM 1601 CA GLN A 274 31.176 27.538 18.095 1.00 21.48 A ATOM 1602 CB GLN A 274 32.323 27.341 17.097 1.00 21.41 A ATOM 1603 Cd GLN A 274 31.934 27.596 15.645 1.00 23.15 A ATOM 1604 CD GLN A 274 33.131 27.588 14.706 1.00 24.80 A ATOM 1605 OE1 GLN A 274 34.276 27.446 15.139 1.00 22.51 A ATOM 1606 NE2 GLN A 274 32.870 27.750 13.413 1.00 22.96 A ATOM 1607 C GLN A 274 30.076 26.517 17.828 1.00 21.51 A ATOM 1608 O GLN A 274 29.123 26.806 17.108 1.00 20.50 A ATOM 1609 N LEU A 275 30.207 25.324 18.403 1.00 21.44 A ATOM 1610 CA LEU A 275 29.196 24.282 18.208 1.00 20.95 A ATOM 1611 CB LEU A 275 29.645 22.958 18.846 1.00 19.11 A ATOM 1612 CG LEU A 275 30.775 22.182 18.159 1.00 21.43 A ATOM 1613 CD1 LEU A 275 31.118 20.936 18.963 1.00 17.64 A ATOM 1614 CD2 LEU A 275 30.342 21.795 16.754 1.00 20.34 A ATOM 1615 C LEU A 275 27.860 24.697 18.815 1.00 21.32 A ATOM 1616 O LEU A 275 26.802 24.461 18.229 1.00 19.75 A ATOM 1617 N VAL A 276 27.921 25.322 19.987 1.00 19.10 A ATOM 1618 CA VAL A 276 26.724 25.750 20.702 1.00 22.47 A ATOM 1619 CB VAL A 276 27.011 25.882 22.217 1.00 20.87 A ATOM 1620 CG1 VAL A 276 25.742 26.291 22.957 1.00 19.68 A ATOM 1621 CG2 VAL A 276 27.550 24.558 22.766 1.00 19.43 A ATOM 1622 C VAL A 276 26.127 27.075 20.211 1.00 23.89 A ATOM 1623 O VAL A 276 24.910 27.199 20.070 1.00 24.90 A ATOM 1624 N ALA A 277 26.983 28.062 19.965 1.00 24.56 A ATOM 1625 CA ALA A 277 26.533 29.374 19.518 1.00 24.72 A ATOM 1626 CB ALA A 277 27.504 30.444 19.999 1.00 24.36 A ATOM 1627 C ALA A 277 26.378 29.458 18.005 1.00 25.76 A ATOM 1628 O ALA A 277 25.577 30.242 17.502 1.00 26.39 A ATOM 1629 N GLY A 278 27.142 28.651 17.280 1.00 25.13 A ATOM 1630 CA GLY A 278 27.062 28.673 15.834 1.00 25.58 A ATOM 1631 C GLY A 278 28.163 29.524 15.231 1.00 26.50 A ATOM 1632 O GLY A 278 28.374 29.510 14.015 1.00 28.17 A ATOM 1633 N LEU A 279 28.866 30.262 16.086 1.00 24.44 A ATOM 1634 CA LEU A 279 29.962 31.130 15.656 1.00 25.21 A ATOM 1635 CB LEU A 279 29.468 32.575 15.500 1.00 25.78 A ATOM 1636 CG LEU A 279 28.364 32.899 14.490 1.00 28.17 A ATOM 1637 CD1 LEU A 279 27.922 34.344 14.684 1.00 26.60 A ATOM 1638 CD2 LEU A 279 28.862 32.670 13.071 1.00 26.52 A ATOM 1639 C LEU A 279 31.093 31.116 16.687 1.00 23.47 A ATOM 1640 O LEU A 279 30.848 30.994 17.882 1.00 24.44 A ATOM 1641 N PRO A 280 32.349 31.239 16.236 1.00 23.35 A ATOM 1642 CD PRO A 280 32.831 31.404 14.855 1.00 22.26 A ATOM 1643 CA PRO A 280 33.464 31.239 17.189 1.00 23.81 A ATOM 1644 CB PRO A 280 34.692 31.293 16.282 1.00 23.24 A ATOM 1645 CG PRO A 280 34.189 32.020 15.073 1.00 24.89 A ATOM 1646 C PRO A 280 33.353 32.444 18.137 1.00 22.69 A ATOM 1647 O PRO A 280 32.750 33.457 17.788 1.00 22.11 A ATOM 1648 N PRO A 281 33.939 32.344 19.345 1.00 23.06 A ATOM 1649 CD PRO A 281 34.810 31.223 19.734 1.00 21.37 A ATOM 1650 CA PRO A 281 33.935 33.375 20.395 1.00 23.67 A ATOM 1651 CB PRO A 281 34.781 32.751 21.509 1.00 24.89 A ATOM 1652 CG PRO A 281 34.749 31.287 21.219 1.00 25.24 A ATOM 1653 C PRO A 281 34.481 34.752 20.017 1.00 23.75 A ATOM 1654 O PRO A 281 33.869 35.781 20.317 1.00 21.02 A ATOM 1655 N PHE A 282 35.644 34.763 19.379 1.00 22.17 A ATOM 1656 CA PHE A 282 36.293 36.007 18.998 1.00 23.16 A ATOM 1657 CB PHE A 282 37.765 35.943 19.406 1.00 21.01 A ATOM 1658 CG PHE A 282 37.975 35.482 20.822 1.00 22.66 A ATOM 1659 CD1 PHE A 282 37.806 36.361 21.888 1.00 20.06 A ATOM 1660 CD2 PHE A 282 38.291 34.151 21.093 1.00 20.72 A ATOM 1661 CEl PHE A 282 37.947 35.921 23.206 1.00 22.66 A ATOM 1662 CE2 PHE A 282 38.433 33.702 22.405 1.00 20.97 A ATOM 1663 CZ PHE A 282 38.261 34.590 23.466 1.00 19.58 A ATOM 1664 C PHE A 282 36.169 36.263 17.503 1.00 24.39 A ATOM 1665 O PHE A 282 36.802 35.585 16.694 1.00 25.80 A ATOM 1666 N ARC A 283 35.355 37.248 17.142 1.00 24.99 A ATOM 1667 CA ARC A 283 35.141 37.594 15.741 1.00 26.33 A ATOM 1668 CB ARC A 283 33.721 37.209 15.316 1.00 28.91 A ATOM 1669 CC ARC A 283 33.293 35.808 15.724 1.00 30.27 A ATOM 1670 CD ARC A 283 31.904 35.493 15.188 1.00 33.36 A ATOM 1671 NE ARC A 283 30.890 36.392 15.733 1.00 32.76 A ATOM 1672 CZ ARC A 283 30.372 36.287 16.952 1.00 34.79 A ATOM 1673 NH1 ARC A 283 30.767 35.317 17.768 1.00 35.77 A ATOM 1674 NH2 ARC A 283 29.458 37.156 17.359 1.00 36.12 A ATOM 1675 C ARC A 283 35.328 39.096 15.544 1.00 26.47 A ATOM 1676 O ARC A 283 35.029 39.888 16.438 1.00 26.28 A ATOM 1677 N ALA A 284 35.818 39.486 14.373 1.00 26.70 A ATOM 1678 CA ALA A 284 36.033 40.899 14.079 1.00 27.84 A ATOM 1679 CB ALA A 284 37.188 41.442 14.914 1.00 26.24 A ATOM 1680 C ALA A 284 36.327 41.077 12.602 1.00 28.35 A ATOM 1681 O ALA A 284 36.560 40.101 11.891 1.00 29.91 A ATOM 1682 N CLY A 285 36.332 42.329 12.153 1.00 29.29 A ATOM 1683 CA CLY A 285 36.577 42.631 10.753 1.00 29.52 A ATOM 1684 C CLY A 285 37.893 42.156 10.168 1.00 30.12 A ATOM 1685 O CLY A 285 37.974 41.862 8.976 1.00 30.60 A ATOM 1686 N ASN A 286 38.939 42.097 10.983 1.00 28.49 A ATOM 1687 CA ASN A 286 40.231 41.644 10.489 1.00 26.71 A ATOM 1688 CB ASN A 286 41.050 42.825 9.945 1.00 26.11 A ATOM 1689 CC ASN A 286 41.310 43.900 10.990 1.00 27.83 A ATOM 1690 OD1 ASN A 286 41.877 43.631 12.049 1.00 27.84 A ATOM 1691 ND2 ASN A 286 40.908 45.131 10.685 1.00 25.95 A ATOM 1692 C ASN A 286 40.997 40.924 11.584 1.00 26.03 A ATOM 1693 O ASN A 286 40.540 40.851 12.723 1.00 25.66 A ATOM 1694 N CLU A 287 42.162 40.391 11.239 1.00 24.81 A ATOM 1695 CA CLU A 287 42.965 39.662 12.206 1.00 27.59 A ATOM 1696 CB CLU A 287 44.145 38.985 11.510 1.00 30.17 A ATOM 1697 CC CLU A 287 43.776 37.632 10.931 1.00 38.21 A ATOM 1698 CD CLU A 287 44.900 36.998 10.140 1.00 41.86 A ATOM 1699 OE1 CLU A 287 46.061 37.036 10.608 1.00 43.08 A ATOM 1700 0E2 CLU A 287 44.612 36.449 9.052 1.00 45.22 A ATOM 1701 C CLU A 287 43.459 40.485 13.383 1.00 25.05 A ATOM 1702 O CLU A 287 43.382 40.030 14.521 1.00 26.41 A ATOM 1703 N TYR A 288 43.966 41.685 13.122 1.00 23.04 A ATOM 1704 CA TYR A 288 44.460 42.528 14.205 1.00 22.34 A ATOM 1705 CB TYR A 288 44.867 43.913 13.691 1.00 21.07 A ATOM 1706 CC TYR A 288 45.275 44.858 14.805 1.00 21.07 A ATOM 1707 CD1 TYR A 288 46.533 44.762 15.405 1.00 21.23 A ATOM 1708 CEl TYR A 288 46.891 45.588 16.475 1.00 20.43 A ATOM 1709 CD2 TYR A 288 44.380 45.809 15.302 1.00 22.32 A ATOM 1710 CE2 TYR A 288 44.725 46.637 16.373 1.00 23.28 A ATOM 1711 CZ TYR A 288 45.981 46.518 16.953 1.00 22.96 A ATOM 1712 OH TYR A 288 46.316 47.313 18.024 1.00 23.18 A ATOM 1713 C TYR A 288 43.402 42.698 15.288 1.00 21.38 A ATOM 1714 O TYR A 288 43.710 42.616 16.473 1.00 22.09 A ATOM 1715 N LEU A 289 42.159 42.939 14.874 1.00 21.88 A ATOM 1716 CA LEU A 289 41.055 43.130 15.811 1.00 21.98 A ATOM 1717 CB LEU A 289 39.821 43.673 15.078 1.00 22.90 A ATOM 1718 CC LEU A 289 39.896 45.130 14.601 1.00 26.52 A ATOM 1719 CD1 LEU A 289 38.706 45.436 13.696 1.00 26.55 A ATOM 1720 CD2 LEU A 289 39.914 46.071 15.807 1.00 23.13 A ATOM 1721 C LEU A 289 40.686 41.849 16.560 1.00 21.24 A ATOM 1722 O LEU A 289 40.256 41.897 17.715 1.00 20.72 A ATOM 1723 N ILE A 290 40.843 40.708 15.900 1.00 19.62 A ATOM 1724 CA ILE A 290 40.538 39.433 16.533 1.00 18.54 A ATOM 1725 CB ILE A 290 40.560 38.281 15.509 1.00 18.52 A ATOM 1726 C02 ILE A 290 40.503 36.934 16.234 1.00 17.63 A ATOM 1727 CCI ILE A 290 39.378 38.429 14.545 1.00 18.88 A ATOM 1728 CD1 ILE A 290 39.421 37.483 13.357 1.00 19.81 A ATOM 1729 C ILE A 290 41.578 39.167 17.618 1.00 19.09 A ATOM 1730 O ILE A 290 41.236 38.788 18.737 1.00 18.20 A ATOM 1731 N PHE A 291 42.849 39.376 17.286 1.00 18.76 A ATOM 1732 CA PHE A 291 43.925 39.156 18.247 1.00 20.75 A ATOM 1733 CB PHE A 291 45.286 39.434 17.606 1.00 20.71 A ATOM 1734 CC PHE A 291 45.644 38.480 16.503 1.00 22.92 A ATOM 1735 CD1 PHE A 291 45.065 37.214 16.443 1.00 22.98 A ATOM 1736 CD2 PHE A 291 46.588 38.830 15.543 1.00 22.91 A ATOM 1737 CEl PHE A 291 45.423 36.310 15.440 1.00 24.51 A ATOM 1738 CE2 PHE A 291 46.954 37.931 14.535 1.00 25.54 A ATOM 1739 CZ PHE A 291 46.370 36.670 14.485 1.00 23.29 A ATOM 1740 C PHE A 291 43.739 40.061 19.451 1.00 21.72 A ATOM 1741 O PHE A 291 43.992 39.671 20.593 1.00 22.32 A ATOM 1742 N GIN A 292 43.284 41.275 19.178 1.00 23.27 A ATOM 1743 CA GIN A 292 43.055 42.264 20.216 1.00 24.01 A ATOM 1744 CB GIN A 292 42.574 43.559 19.562 1.00 25.77 A ATOM 1745 CC GIN A 292 42.577 44.773 20.447 1.00 28.45 A ATOM 1746 CD GIN A 292 42.469 46.057 19.638 1.00 29.83 A ATOM 1747 OE1 GIN A 292 41.520 46.244 18.872 1.00 27.16 A ATOM 1748 NE2 GIN A 292 43.449 46.944 19.799 1.00 27.61 A ATOM 1749 C GIN A 292 42.018 41.733 21.204 1.00 22.97 A ATOM 1750 O GIN A 292 42.200 41.832 22.415 1.00 21.64 A ATOM 1751 N LYS A 293 40.937 41.154 20.687 1.00 21.82 A ATOM 1752 CA LYS A 293 39.895 40.612 21.558 1.00 22.18 A ATOM 1753 CB LYS A 293 38.664 40.223 20.740 1.00 22.69 A ATOM 1754 CC LYS A 293 37.919 41.407 20.153 1.00 25.78 A ATOM 1755 CD LYS A 293 36.651 40.961 19.429 1.00 27.88 A ATOM 1756 CE LYS A 293 35.857 42.161 18.926 1.00 30.85 A ATOM 1757 NZ LYS A 293 34.612 41.750 18.214 1.00 32.98 A ATOM 1758 C LYS A 293 40.398 39.398 22.343 1.00 21.20 A ATOM 1759 O LYS A 293 40.041 39.204 23.509 1.00 22.01 A ATOM 1760 N ILE A 294 41.226 38.583 21.702 1.00 19.91 A ATOM 1761 CA ILE A 294 41.774 37.394 22.347 1.00 20.28 A ATOM 1762 CB ILE A 294 42.631 36.575 21.349 1.00 18.98 A ATOM 1763 CC2 ILE A 294 43.481 35.550 22.098 1.00 17.70 A ATOM 1764 CCI ILE A 294 41.716 35.897 20.318 1.00 17.93 A ATOM 1765 CD1 ILE A 294 42.467 35.237 19.178 1.00 16.21 A ATOM 1766 C ILE A 294 42.618 37.727 23.587 1.00 21.94 A ATOM 1767 O ILE A 294 42.366 37.199 24.673 1.00 20.86 A ATOM 1768 N ILE A 295 43.610 38.600 23.439 1.00 21.88 A ATOM 1769 CA ILE A 295 44.461 38.934 24.582 1.00 24.25 A ATOM 1770 CB ILE A 295 45.668 39.805 24.175 1.00 23.93 A ATOM 1771 CC2 ILE A 295 46.514 39.066 23.140 1.00 24.61 A ATOM 1772 CCI ILE A 295 45.189 41.151 23.637 1.00 24.58 A ATOM 1773 CD1 ILE A 295 46.317 42.149 23.433 1.00 26.69 A ATOM 1774 C ILE A 295 43.720 39.636 25.717 1.00 24.80 A ATOM 1775 O ILE A 295 44.214 39.687 26.842 1.00 24.76 A ATOM 1776 N LYS A 296 42.539 40.173 25.425 1.00 25.33 A ATOM 1777 CA LYS A 296 41.743 40.853 26.444 1.00 26.80 A ATOM 1778 CB LYS A 296 41.178 42.170 25.894 1.00 27.39 A ATOM 1779 CC LYS A 296 42.240 43.141 25.413 1.00 31.79 A ATOM 1780 CD LYS A 296 41.634 44.410 24.826 1.00 35.56 A ATOM 1781 CE LYS A 296 41.009 45.283 25.900 1.00 39.29 A ATOM 1782 NZ LYS A 296 40.564 46.603 25.357 1.00 41.72 A ATOM 1783 C LYS A 296 40.593 39.958 26.893 1.00 25.50 A ATOM 1784 O LYS A 296 39.770 40.361 27.713 1.00 24.02 A ATOM 1785 N LEU A 297 40.550 38.742 26.349 1.00 25.67 A ATOM 1786 CA LEU A 297 39.500 37.777 26.666 1.00 25.16 A ATOM 1787 CB LEU A 297 39.632 37.285 28.111 1.00 24.80 A ATOM 1788 CG LEU A 297 38.766 36.068 28.460 1.00 26.43 A ATOM 1789 CD1 LEU A 297 39.238 34.852 27.646 1.00 26.70 A ATOM 1790 CD2 LEU A 297 38.856 35.777 29.951 1.00 24.84 A ATOM 1791 C LEU A 297 38.151 38.459 26.467 1.00 25.11 A ATOM 1792 O LEU A 297 37.261 38.378 27.309 1.00 25.28 A ATOM 1793 N GLU A 298 38.007 39.127 25.331 1.00 24.98 A ATOM 1794 CA GLU A 298 36.786 39.847 25.023 1.00 25.31 A ATOM 1795 CB GLU A 298 37.143 41.139 24.291 1.00 27.13 A ATOM 1796 CG GLU A 298 35.991 42.092 24.108 1.00 31.28 A ATOM 1797 CD GLU A 298 36.419 43.362 23.410 1.00 34.40 A ATOM 1798 OE1 GLU A 298 37.348 44.027 23.918 1.00 35.90 A ATOM 1799 OE2 GLU A 298 35.832 43.693 22.359 1.00 36.16 A ATOM 1800 C GLU A 298 35.766 39.057 24.207 1.00 23.79 A ATOM 1801 O GLU A 298 35.832 39.017 22.979 1.00 24.35 A ATOM 1802 N TYR A 299 34.825 38.427 24.902 1.00 23.45 A ATOM 1803 CA TYR A 299 33.760 37.663 24.265 1.00 23.98 A ATOM 1804 CB TYR A 299 34.264 36.304 23.755 1.00 20.13 A ATOM 1805 CG TYR A 299 34.348 35.233 24.828 1.00 21.17 A ATOM 1806 CD1 TYR A 299 35.336 35.279 25.810 1.00 19.32 A ATOM 1807 CEl TYR A 299 35.389 34.332 26.826 1.00 19.30 A ATOM 1808 CD2 TYR A 299 33.410 34.201 24.888 1.00 18.96 A ATOM 1809 CE2 TYR A 299 33.456 33.243 25.907 1.00 19.41 A ATOM 1810 CZ TYR A 299 34.449 33.321 26.870 1.00 18.79 A ATOM 1811 OH TYR A 299 34.511 32.401 27.881 1.00 18.77 A ATOM 1812 C TYR A 299 32.699 37.437 25.331 1.00 25.20 A ATOM 1813 O TYR A 299 32.942 37.681 26.506 1.00 26.46 A ATOM 1814 N ASP A 300 31.522 36.981 24.927 1.00 26.94 A ATOM 1815 CA ASP A 300 30.467 36.710 25.891 1.00 30.60 A ATOM 1816 CB ASP A 300 29.665 37.981 26.179 1.00 35.86 A ATOM 1817 CG ASP A 300 29.228 38.687 24.923 1.00 42.04 A ATOM 1818 ODi ASP A 300 28.450 38.088 24.149 1.00 45.98 A ATOM 1819 0D2 ASP A 300 29.666 39.840 24.707 1.00 45.69 A ATOM 1820 C ASP A 300 29.564 35.608 25.363 1.00 29.26 A ATOM 1821 O ASP A 300 29.590 35.299 24.172 1.00 28.64 A ATOM 1822 N PHE A 301 28.778 35.011 26.253 1.00 28.96 A ATOM 1823 CA PHE A 301 27.884 33.924 25.871 1.00 30.48 A ATOM 1824 CB PHE A 301 27.818 32.854 26.968 1.00 29.17 A ATOM 1825 CG PHE A 301 29.147 32.279 27.356 1.00 29.29 A ATOM 1826 CD1 PHE A 301 29.978 32.949 28.245 1.00 27.31 A ATOM 1827 CD2 PHE A 301 29.560 31.050 26.845 1.00 27.89 A ATOM 1828 CEl PHE A 301 31.205 32.403 28.625 1.00 28.83 A ATOM 1829 CE2 PHE A 301 30.781 30.498 27.217 1.00 28.05 A ATOM 1830 CZ PHE A 301 31.605 31.175 28.110 1.00 28.27 A ATOM 1831 C PHE A 301 26.459 34.384 25.619 1.00 32.20 A ATOM 1832 O PHE A 301 25.946 35.261 26.317 1.00 32.36 A ATOM 1833 N PRO A 302 25.798 33.804 24.607 1.00 33.29 A ATOM 1834 CD PRO A 302 26.313 32.943 23.529 1.00 34.04 A ATOM 1835 CA PRO A 302 24.415 34.199 24.341 1.00 35.24 A ATOM 1836 CB PRO A 302 24.144 33.608 22.959 1.00 34.01 A ATOM 1837 CG PRO A 302 25.041 32.413 22.921 1.00 35.48 A ATOM 1838 C PRO A 302 23.567 33.561 25.444 1.00 37.39 A ATOM 1839 O PRO A 302 23.935 32.518 25.986 1.00 38.49 A ATOM 1840 N ALA A 303 22.447 34.188 25.783 1.00 39.36 A ATOM 1841 CA ALA A 303 21.572 33.692 26.843 1.00 40.65 A ATOM 1842 CB ALA A 303 20.280 34.506 26.862 1.00 41.66 A ATOM 1843 C ALA A 303 21.238 32.197 26.814 1.00 41.25 A ATOM 1844 O ALA A 303 21.253 31.537 27.854 1.00 43.16 A ATOM 1845 N ALA A 304 20.945 31.665 25.631 1.00 41.04 A ATOM 1846 CA ALA A 304 20.569 30.258 25.480 1.00 40.66 A ATOM 1847 CB ALA A 304 20.121 30.004 24.040 1.00 41.36 A ATOM 1848 C ALA A 304 21.628 29.223 25.876 1.00 39.61 A ATOM 1849 O ALA A 304 21.298 28.156 26.395 1.00 40.61 A ATOM 1850 N PHE A 305 22.891 29.543 25.617 1.00 36.21 A ATOM 1851 CA PHE A 305 24.022 28.662 25.909 1.00 32.08 A ATOM 1852 CB PHE A 305 25.259 29.519 26.187 1.00 29.46 A ATOM 1853 CG PHE A 305 26.536 28.917 25.690 1.00 28.15 A ATOM 1854 CD1 PHE A 305 27.146 27.875 26.377 1.00 26.20 A ATOM 1855 CD2 PHE A 305 27.127 29.386 24.521 1.00 27.05 A ATOM 1856 CEl PHE A 305 28.330 27.308 25.908 1.00 26.92 A ATOM 1857 CE2 PHE A 305 28.312 28.826 24.042 1.00 26.62 A ATOM 1858 CZ PHE A 305 28.914 27.786 24.737 1.00 26.61 A ATOM 1859 C PHE A 305 23.811 27.664 27.057 1.00 30.09 A ATOM 1860 O PHE A 305 23.518 28.051 28.187 1.00 31.51 A ATOM 1861 N PHE A 306 23.964 26.378 26.758 1.00 27.01 A ATOM 1862 CA PHE A 306 23.801 25.334 27.769 1.00 26.30 A ATOM 1863 CB PHE A 306 24.157 23.970 27.170 1.00 25.03 A ATOM 1864 CG PHE A 306 23.548 23.725 25.815 1.00 27.24 A ATOM 1865 CD1 PHE A 306 22.170 23.831 25.622 1.00 28.40 A ATOM 1866 CD2 PHE A 306 24.350 23.386 24.728 1.00 27.84 A ATOM 1867 CEl PHE A 306 21.601 23.603 24.365 1.00 28.05 A ATOM 1868 CE2 PHE A 306 23.792 23.155 23.465 1.00 28.31 A ATOM 1869 CZ PHE A 306 22.415 23.263 23.283 1.00 28.00 A ATOM 1870 C PHE A 306 24.711 25.652 28.961 1.00 26.23 A ATOM 1871 O PHE A 306 25.927 25.775 28.811 1.00 25.59 A ATOM 1872 N PRO A 307 24.125 25.796 30.163 1.00 26.67 A ATOM 1873 CD PRO A 307 22.685 25.625 30.430 1.00 27.95 A ATOM 1874 CA PRO A 307 24.842 26.110 31.405 1.00 26.59 A ATOM 1875 CB PRO A 307 23.795 25.832 32.481 1.00 26.14 A ATOM 1876 CG PRO A 307 22.531 26.250 31.803 1.00 27.86 A ATOM 1877 C PRO A 307 26.145 25.355 31.659 1.00 25.58 A ATOM 1878 O PRO A 307 27.189 25.964 31.900 1.00 22.65 A ATOM 1879 N LYS A 308 26.085 24.031 31.620 1.00 24.46 A ATOM 1880 CA LYS A 308 27.274 23.232 31.867 1.00 23.91 A ATOM 1881 CB LYS A 308 26.887 21.760 32.024 1.00 23.25 A ATOM 1882 CG LYS A 308 26.062 21.532 33.285 1.00 28.49 A ATOM 1883 CD LYS A 308 25.618 20.093 33.466 1.00 30.17 A ATOM 1884 CE LYS A 308 24.760 19.973 34.722 1.00 33.12 A ATOM 1885 NZ LYS A 308 24.122 18.636 34.860 1.00 34.13 A ATOM 1886 C LYS A 308 28.314 23.426 30.769 1.00 22.84 A ATOM 1887 O LYS A 308 29.514 23.411 31.042 1.00 22.46 A ATOM 1888 N ALA A 309 27.861 23.621 29.534 1.00 21.59 A ATOM 1889 CA ALA A 309 28.792 23.848 28.432 1.00 20.02 A ATOM 1890 CB ALA A 309 28.056 23.856 27.106 1.00 18.80 A ATOM 1891 C ALA A 309 29.481 25.191 28.662 1.00 21.41 A ATOM 1892 O ALA A 309 30.680 25.335 28.427 1.00 21.39 A ATOM 1893 N ARG A 310 28.717 26.179 29.121 1.00 21.39 A ATOM 1894 CA ARG A 310 29.290 27.494 29.388 1.00 22.02 A ATOM 1895 CB ARG A 310 28.213 28.479 29.854 1.00 22.39 A ATOM 1896 CG ARG A 310 28.806 29.756 30.436 1.00 25.30 A ATOM 1897 CD ARG A 310 27.780 30.852 30.664 1.00 28.33 A ATOM 1898 NE ARG A 310 28.420 32.039 31.230 1.00 30.18 A ATOM 1899 CZ ARG A 310 27.901 33.263 31.203 1.00 32.07 A ATOM 1900 NH1 ARG A 310 26.719 33.477 30.634 1.00 31.19 A ATOM 1901 NH2 ARG A 310 28.567 34.277 31.742 1.00 30.49 A ATOM 1902 C ARG A 310 30.376 27.388 30.458 1.00 21.65 A ATOM 1903 O ARG A 310 31.464 27.949 30.311 1.00 20.36 A ATOM 1904 N ASP A 311 30.074 26.677 31.541 1.00 19.57 A ATOM 1905 CA ASP A 311 31.043 26.512 32.615 1.00 20.18 A ATOM 1906 CB ASP A 311 30.460 25.649 33.739 1.00 20.39 A ATOM 1907 CG ASP A 311 31.439 25.446 34.881 1.00 23.35 A ATOM 1908 OD1 ASP A 311 32.158 24.428 34.885 1.00 24.91 A ATOM 1909 OD2 ASP A 311 31.500 26.312 35.776 1.00 26.96 A ATOM 1910 C ASP A 311 32.322 25.877 32.073 1.00 19.73 A ATOM 1911 O ASP A 311 33.422 26.289 32.439 1.00 19.30 A ATOM 1912 N LEU A 312 32.179 24.891 31.188 1.00 16.32 A ATOM 1913 CA LEU A 312 33.349 24.226 30.611 1.00 16.66 A ATOM 1914 CB LEU A 312 32.927 23.035 29.744 1.00 16.12 A ATOM 1915 CG LEU A 312 34.050 22.320 28.974 1.00 14.73 A ATOM 1916 CD1 LEU A 312 35.192 21.935 29.912 1.00 14.56 A ATOM 1917 CD2 LEU A 312 33.477 21.084 28.289 1.00 14.22 A ATOM 1918 C LEU A 312 34.181 25.189 29.774 1.00 16.61 A ATOM 1919 O LEU A 312 35.402 25.241 29.910 1.00 16.20 A ATOM 1920 N VAL A 313 33.515 25.949 28.908 1.00 16.20 A ATOM 1921 CA VAL A 313 34.207 26.907 28.058 1.00 15.37 A ATOM 1922 CB VAL A 313 33.216 27.648 27.130 1.00 16.42 A ATOM 1923 CG1 VAL A 313 33.915 28.796 26.426 1.00 16.93 A ATOM 1924 CG2 VAL A 313 32.644 26.672 26.103 1.00 17.88 A ATOM 1925 C VAL A 313 34.960 27.923 28.911 1.00 17.39 A ATOM 1926 O VAL A 313 36.093 28.294 28.591 1.00 18.00 A ATOM 1927 N GLU A 314 34.342 28.364 30.004 1.00 17.61 A ATOM 1928 CA GLU A 314 34.986 29.331 30.885 1.00 20.43 A ATOM 1929 CB GLU A 314 34.009 29.816 31.959 1.00 22.14 A ATOM 1930 CG GLU A 314 32.800 30.550 31.396 1.00 26.52 A ATOM 1931 CD GLU A 314 31.852 31.025 32.478 1.00 31.26 A ATOM 1932 OE1 GLU A 314 31.580 30.246 33.417 1.00 33.48 A ATOM 1933 OE2 GLU A 314 31.370 32.173 32.387 1.00 34.81 A ATOM 1934 C GLU A 314 36.217 28.721 31.539 1.00 19.15 A ATOM 1935 O GLU A 314 37.134 29.433 31.934 1.00 21.47 A ATOM 1936 N LYS A 315 36.245 27.400 31.651 1.00 19.51 A ATOM 1937 CA LYS A 315 37.394 26.749 32.258 1.00 19.17 A ATOM 1938 CB LYS A 315 36.946 25.514 33.043 1.00 18.84 A ATOM 1939 CG LYS A 315 36.280 25.885 34.368 1.00 19.62 A ATOM 1940 CD LYS A 315 35.653 24.696 35.073 1.00 19.22 A ATOM 1941 CE LYS 315 35.070 25.095 36.427 0.50 21.00 AC1 ATOM 1942 NZ LYS 315 36.119 25.552 37.381 0.50 19.53 AC1 ATOM 1943 C LYS A 315 38.452 26.393 31.218 1.00 18.96 A ATOM 1944 O LYS A 315 39.511 25.873 31.561 1.00 19.85 A ATOM 1945 N LEU A 316 38.164 26.691 29.950 1.00 17.08 A ATOM 1946 CA LEU A 316 39.102 26.429 28.854 1.00 16.41 A ATOM 1947 CB LEU A 316 38.414 25.636 27.738 1.00 13.81 A ATOM 1948 CG LEU A 316 38.028 24.201 28.115 1.00 14.39 A ATOM 1949 CD1 LEU A 316 37.139 23.597 27.031 1.00 12.38 A ATOM 1950 CD2 LEU A 316 39.302 23.373 28.309 1.00 12.77 A ATOM 1951 C LEU A 316 39.652 27.743 28.290 1.00 17.12 A ATOM 1952 O LEU A 316 40.851 27.860 28.023 1.00 16.53 A ATOM 1953 N LEU A 317 38.780 28.729 28.105 1.00 16.27 A ATOM 1954 CA LEU A 317 39.228 30.022 27.596 1.00 17.52 A ATOM 1955 CB LEU A 317 38.083 30.752 26.887 1.00 16.37 A ATOM 1956 CG LEU A 317 37.448 29.973 25.727 1.00 18.81 A ATOM 1957 CD1 LEU A 317 36.415 30.851 25.018 1.00 16.47 A ATOM 1958 CD2 LEU A 317 38.528 29.526 24.741 1.00 17.87 A ATOM 1959 C LEU A 317 39.745 30.841 28.774 1.00 18.27 A ATOM 1960 O LEU A 317 39.078 31.753 29.273 1.00 18.58 A ATOM 1961 N VAL A 318 40.937 30.475 29.229 1.00 18.02 A ATOM 1962 CA VAL A 318 41.593 31.141 30.342 1.00 18.85 A ATOM 1963 CB VAL A 318 41.846 30.153 31.500 1.00 19.91 A ATOM 1964 CG1 VAL A 318 42.590 30.848 32.634 1.00 20.01 A ATOM 1965 CG2 VAL A 318 40.520 29.584 31.990 1.00 19.44 A ATOM 1966 C VAL A 318 42.923 31.657 29.811 1.00 19.67 A ATOM 1967 O VAL A 318 43.690 30.902 29.208 1.00 18.26 A ATOM 1968 N LEU A 319 43.197 32.939 30.028 1.00 20.07 A ATOM 1969 CA LEU A 319 44.436 33.533 29.538 1.00 20.98 A ATOM 1970 CB LEU A 319 44.521 35.002 29.968 1.00 21.64 A ATOM 1971 CG LEU A 319 43.418 35.908 29.408 1.00 24.38 A ATOM 1972 CD1 LEU A 319 43.606 37.332 29.935 1.00 23.28 A ATOM 1973 CD2 LEU A 319 43.453 35.887 27.875 1.00 24.33 A ATOM 1974 C LEU A 319 45.680 32.774 29.994 1.00 20.38 A ATOM 1975 O LEU A 319 46.568 32.496 29.192 1.00 21.34 A ATOM 1976 N ASP A 320 45.742 32.440 31.280 1.00 20.22 A ATOM 1977 CA ASP A 320 46.879 31.707 31.833 1.00 20.90 A ATOM 1978 CB ASP A 320 46.842 31.760 33.365 1.00 20.76 A ATOM 1979 CG ASP A 320 48.049 31.102 34.004 1.00 21.51 A ATOM 1980 OD1 ASP A 320 48.669 30.226 33.367 1.00 23.46 A ATOM 1981 OD2 ASP A 320 48.371 31.450 35.159 1.00 23.89 A ATOM 1982 C ASP A 320 46.814 30.247 31.367 1.00 20.06 A ATOM 1983 O ASP A 320 45.988 29.476 31.840 1.00 20.54 A ATOM 1984 N ALA A 321 47.700 29.876 30.451 1.00 20.68 A ATOM 1985 CA ALA A 321 47.733 28.522 29.903 1.00 22.04 A ATOM 1986 CB ALA A 321 48.860 28.411 28.881 1.00 20.75 A ATOM 1987 C ALA A 321 47.858 27.400 30.940 1.00 21.62 A ATOM 1988 O ALA A 321 47.482 26.259 30.665 1.00 21.99 A ATOM 1989 N THR A 322 48.372 27.715 32.127 1.00 20.89 A ATOM 1990 CA THR A 322 48.531 26.698 33.167 1.00 20.82 A ATOM 1991 CB THR A 322 49.670 27.051 34.146 1.00 19.47 A ATOM 1992 OG1 THR A 322 49.341 28.253 34.848 1.00 20.19 A ATOM 1993 CG2 THR A 322 50.981 27.249 33.394 1.00 21.59 A ATOM 1994 C THR A 322 47.264 26.498 33.983 1.00 19.55 A ATOM 1995 O THR A 322 47.235 25.673 34.894 1.00 21.13 A ATOM 1996 N LYS A 323 46.216 27.248 33.661 1.00 19.33 A ATOM 1997 CA LYS A 323 44.962 27.122 34.392 1.00 21.20 A ATOM 1998 CB LYS A 323 44.580 28.460 35.030 1.00 23.75 A ATOM 1999 CG LYS A 323 45.562 28.933 36.084 1.00 28.45 A ATOM 2000 CD LYS A 323 45.055 30.177 36.799 1.00 33.76 A ATOM 2001 CE LYS A 323 46.087 30.678 37.802 1.00 36.15 A ATOM 2002 NZ LYS A 323 46.532 29.569 38.693 1.00 37.34 A ATOM 2003 C LYS A 323 43.806 26.614 33.539 1.00 20.68 A ATOM 2004 O LYS A 323 42.649 26.757 33.915 1.00 20.42 A ATOM 2005 N ARG A 324 44.114 26.019 32.392 1.00 19.97 A ATOM 2006 CA ARG A 324 43.060 25.494 31.531 1.00 17.98 A ATOM 2007 CB ARG A 324 43.461 25.609 30.061 1.00 15.95 A ATOM 2008 CG ARG A 324 43.534 27.050 29.603 1.00 17.34 A ATOM 2009 CD ARG A 324 43.996 27.194 28.172 1.00 19.80 A ATOM 2010 NE ARG A 324 44.438 28.565 27.944 1.00 16.93 A ATOM 2011 CZ ARG A 324 45.410 28.908 27.108 1.00 19.88 A ATOM 2012 NH1 ARG A 324 46.045 27.978 26.398 1.00 14.58 A ATOM 2013 NH2 ARG A 324 45.774 30.181 27.015 1.00 16.51 A ATOM 2014 C ARG A 324 42.762 24.046 31.883 1.00 18.32 A ATOM 2015 O ARG A 324 43.673 23.222 32.006 1.00 18.20 A ATOM 2016 N LEU A 325 41.479 23.748 32.055 1.00 18.32 A ATOM 2017 CA LEU A 325 41.050 22.403 32.395 1.00 17.79 A ATOM 2018 CB LEU A 325 39.523 22.335 32.425 1.00 17.03 A ATOM 2019 CG LEU A 325 38.896 21.125 33.116 1.00 15.91 A ATOM 2020 CD1 LEU A 325 39.392 21.048 34.557 1.00 15.93 A ATOM 2021 CD2 LEU A 325 37.375 21.255 33.084 1.00 16.56 A ATOM 2022 C LEU A 325 41.599 21.433 31.356 1.00 18.68 A ATOM 2023 O LEU A 325 41.347 21.586 30.157 1.00 18.28 A ATOM 2024 N GLY A 326 42.354 20.439 31.821 1.00 18.18 A ATOM 2025 CA GLY A 326 42.931 19.462 30.915 1.00 16.36 A ATOM 2026 C GLY A 326 44.443 19.558 30.807 1.00 19.15 A ATOM 2027 O GLY A 326 45.093 18.592 30.404 1.00 19.52 A ATOM 2028 N CYS A 327 45.016 20.708 31.161 1.00 18.16 A ATOM 2029 CA CYS A 327 46.463 20.867 31.075 1.00 19.30 A ATOM 2030 CB CYS A 327 46.856 22.350 31.058 1.00 20.22 A ATOM 2031 SG CYS A 327 46.782 23.200 32.649 1.00 21.97 A ATOM 2032 C CYS A 327 47.169 20.157 32.228 1.00 20.22 A ATOM 2033 O CYS A 327 46.561 19.828 33.246 1.00 17.92 A ATOM 2034 N GLU A 328 48.463 19.933 32.053 1.00 20.51 A ATOM 2035 CA GLU A 328 49.274 19.244 33.042 1.00 23.34 A ATOM 2036 CB GLU A 328 50.710 19.139 32.507 1.00 28.68 A ATOM 2037 CG GLU A 328 50.754 18.367 31.175 1.00 38.24 A ATOM 2038 CD GLU A 328 52.067 18.500 30.414 1.00 43.23 A ATOM 2039 OE1 GLU A 328 52.535 19.643 30.218 1.00 46.22 A ATOM 2040 0E2 GLU A 328 52.618 17.459 29.991 1.00 44.90 A ATOM 2041 C GLU A 328 49.234 19.876 34.435 1.00 22.11 A ATOM 2042 O GLU A 328 49.147 19.161 35.437 1.00 20.27 A ATOM 2043 N GLU A 329 49.276 21.204 34.506 1.00 18.40 A ATOM 2044 CA GLU A 329 49.248 21.875 35.801 1.00 20.13 A ATOM 2045 CB GLU A 329 49.587 23.363 35.657 1.00 20.36 A ATOM 2046 CG GLU A 329 51.014 23.651 35.190 1.00 24.05 A ATOM 2047 CD GLU A 329 51.191 23.518 33.688 1.00 25.93 A ATOM 2048 OE1 GLU A 329 50.213 23.154 32.995 1.00 26.61 A ATOM 2049 0E2 GLU A 329 52.311 23.781 33.198 1.00 27.19 A ATOM 2050 C GLU A 329 47.890 21.718 36.480 1.00 19.36 A ATOM 2051 O GLU A 329 47.775 21.879 37.694 1.00 18.74 A ATOM 2052 N MET A 330 46.863 21.415 35.691 1.00 17.28 A ATOM 2053 CA MET A 330 45.520 21.220 36.229 1.00 16.38 A ATOM 2054 CB MET A 330 44.474 21.833 35.294 1.00 17.65 A ATOM 2055 CG MET A 330 44.460 23.365 35.311 1.00 22.95 A ATOM 2056 SD MET A 330 44.186 24.026 36.979 1.00 26.78 A ATOM 2057 CE MET A 330 42.435 23.712 37.186 1.00 24.69 A ATOM 2058 C MET A 330 45.257 19.730 36.422 1.00 14.30 A ATOM 2059 O MET A 330 44.127 19.304 36.629 1.00 15.39 A ATOM 2060 N GLU A 331 46.327 18.949 36.346 1.00 15.60 A ATOM 2061 CA GLU A 331 46.289 17.501 36.531 1.00 17.08 A ATOM 2062 CB GLU A 331 45.607 17.155 37.862 1.00 17.00 A ATOM 2063 CG GLU A 331 46.070 18.027 39.038 1.00 17.46 A ATOM 2064 CD GLU A 331 47.591 18.179 39.145 1.00 20.16 A ATOM 2065 OE1 GLU A 331 48.034 19.073 39.896 1.00 21.39 A ATOM 2066 0E2 GLU A 331 48.345 17.420 38.500 1.00 18.87 A ATOM 2067 C GLU A 331 45.697 16.658 35.398 1.00 17.80 A ATOM 2068 O GLU A 331 45.107 15.602 35.636 1.00 20.40 A ATOM 2069 N GLY A 332 45.844 17.133 34.167 1.00 16.23 A ATOM 2070 CA GLY A 332 45.420 16.353 33.015 1.00 14.10 A ATOM 2071 C GLY A 332 43.982 16.154 32.596 1.00 13.54 A ATOM 2072 O GLY A 332 43.063 16.864 33.017 1.00 11.96 A ATOM 2073 N TYR A 333 43.804 15.141 31.750 1.00 14.37 A ATOM 2074 CA TYR A 333 42.510 14.806 31.182 1.00 13.56 A ATOM 2075 CB TYR A 333 42.722 13.892 29.968 1.00 15.00 A ATOM 2076 CG TYR A 333 43.153 14.683 28.752 1.00 16.46 A ATOM 2077 CD1 TYR A 333 42.206 15.172 27.849 1.00 15.29 A ATOM 2078 CEl TYR A 333 42.573 16.002 26.794 1.00 13.42 A ATOM 2079 CD2 TYR A 333 44.490 15.039 28.561 1.00 14.91 A ATOM 2080 CE2 TYR A 333 44.872 15.877 27.499 1.00 14.87 A ATOM 2081 CZ TYR A 333 43.902 16.353 26.626 1.00 15.61 A ATOM 2082 OH TYR A 333 44.244 17.197 25.599 1.00 17.29 A ATOM 2083 C TYR A 333 41.470 14.230 32.127 1.00 15.23 A ATOM 2084 O TYR A 333 40.278 14.323 31.846 1.00 16.63 A ATOM 2085 N GLY A 334 41.907 13.650 33.244 1.00 15.50 A ATOM 2086 CA GLY A 334 40.957 13.100 34.202 1.00 15.07 A ATOM 2087 C GLY A 334 39.925 14.146 34.616 1.00 16.40 A ATOM 2088 O GLY A 334 38.724 13.946 34.433 1.00 15.05 A ATOM 2089 N PRO A 335 40.366 15.278 35.184 1.00 14.96 A ATOM 2090 CD PRO A 335 41.727 15.531 35.689 1.00 15.88 A ATOM 2091 CA PRO A 335 39.444 16.339 35.606 1.00 15.29 A ATOM 2092 CB PRO A 335 40.383 17.397 36.178 1.00 13.19 A ATOM 2093 CG PRO A 335 41.485 16.569 36.758 1.00 13.81 A ATOM 2094 C PRO A 335 38.594 16.877 34.448 1.00 15.84 A ATOM 2095 O PRO A 335 37.423 17.204 34.631 1.00 14.84 A ATOM 2096 N LEU A 336 39.184 16.971 33.257 1.00 16.12 A ATOM 2097 CA LEU A 336 38.450 17.465 32.094 1.00 15.52 A ATOM 2098 CB LEU A 336 39.396 17.653 30.898 1.00 14.39 A ATOM 2099 CG LEU A 336 38.770 17.991 29.538 1.00 15.46 A ATOM 2100 CD1 LEU A 336 37.836 19.182 29.662 1.00 11.25 A ATOM 2101 CD2 LEU A 336 39.884 18.285 28.528 1.00 14.11 A ATOM 2102 C LEU A 336 37.321 16.508 31.714 1.00 16.28 A ATOM 2103 O LEU A 336 36.176 16.921 31.540 1.00 15.51 A ATOM 2104 N LYS A 337 37.640 15.225 31.592 1.00 17.22 A ATOM 2105 CA LYS A 337 36.624 14.243 31.235 1.00 17.39 A ATOM 2106 CB LYS A 337 37.293 12.900 30.921 1.00 17.68 A ATOM 2107 CG LYS A 337 38.170 12.994 29.676 1.00 22.31 A ATOM 2108 CD LYS A 337 39.213 11.892 29.592 1.00 24.60 A ATOM 2109 CE LYS A 337 38.620 10.560 29.189 1.00 24.76 A ATOM 2110 NZ LYS A 337 39.710 9.560 28.997 1.00 25.05 A ATOM 2111 C LYS A 337 35.577 14.096 32.342 1.00 17.33 A ATOM 2112 O LYS A 337 34.456 13.652 32.090 1.00 14.42 A ATOM 2113 N ALA A 338 35.928 14.500 33.559 1.00 15.83 A ATOM 2114 CA ALA A 338 34.989 14.395 34.674 1.00 17.52 A ATOM 2115 CB ALA A 338 35.749 14.167 35.980 1.00 19.68 A ATOM 2116 C ALA A 338 34.095 15.621 34.804 1.00 18.83 A ATOM 2117 O ALA A 338 33.252 15.687 35.695 1.00 18.94 A ATOM 2118 N HIS A 339 34.262 16.596 33.918 1.00 19.42 A ATOM 2119 CA HIS A 339 33.438 17.796 34.004 1.00 19.28 A ATOM 2120 CB HIS A 339 33.865 18.819 32.949 1.00 19.20 A ATOM 2121 CG HIS A 339 33.163 20.134 33.074 1.00 20.26 A ATOM 2122 CD2 HIS A 339 33.549 21.299 33.649 1.00 18.95 A ATOM 2123 ND1 HIS A 339 31.880 20.340 32.612 1.00 19.10 A ATOM 2124 CEl HIS A 339 31.506 21.576 32.896 1.00 22.19 A ATOM 2125 NE2 HIS A 339 32.500 22.179 33.525 1.00 21.98 A ATOM 2126 C HIS A 339 31.957 17.448 33.845 1.00 19.13 A ATOM 2127 O HIS A 339 31.597 16.576 33.061 1.00 19.52 A ATOM 2128 N PRO A 340 31.079 18.125 34.606 1.00 19.80 A ATOM 2129 CD PRO A 340 31.424 19.119 35.640 1.00 19.08 A ATOM 2130 CA PRO A 340 29.630 17.900 34.569 1.00 20.52 A ATOM 2131 CB PRO A 340 29.091 19.058 35.396 1.00 20.74 A ATOM 2132 CG PRO A 340 30.146 19.207 36.454 1.00 19.20 A ATOM 2133 C PRO A 340 29.000 17.834 33.176 1.00 21.42 A ATOM 2134 O PRO A 340 28.049 17.088 32.955 1.00 22.48 A ATOM 2135 N PHE A 341 29.528 18.606 32.237 1.00 21.33 A ATOM 2136 CA PHE A 341 28.985 18.610 30.886 1.00 21.57 A ATOM 2137 CB PHE A 341 29.739 19.624 30.017 1.00 21.64 A ATOM 2138 CC PHE A 341 29.207 19.740 28.613 1.00 23.18 A ATOM 2139 CD1 PHE A 341 27.903 20.171 28.382 1.00 22.58 A ATOM 2140 CD2 PHE A 341 30.013 19.431 27.522 1.00 21.95 A ATOM 2141 CEl PHE A 341 27.410 20.292 27.082 1.00 23.54 A ATOM 2142 CE2 PHE A 341 29.533 19.548 26.220 1.00 21.83 A ATOM 2143 CZ PHE A 341 28.228 19.980 25.998 1.00 23.23 A ATOM 2144 C PHE A 341 29.055 17.226 30.237 1.00 21.84 A ATOM 2145 O PHE A 341 28.232 16.896 29.389 1.00 20.37 A ATOM 2146 N PHE A 342 30.034 16.422 30.640 1.00 20.51 A ATOM 2147 CA PHE A 342 30.221 15.085 30.077 1.00 23.01 A ATOM 2148 CB PHE A 342 31.710 14.809 29.850 1.00 18.00 A ATOM 2149 CC PHE A 342 32.398 15.812 28.971 1.00 17.05 A ATOM 2150 CD1 PHE A 342 32.010 15.987 27.652 1.00 17.78 A ATOM 2151 CD2 PHE A 342 33.487 16.534 29.450 1.00 15.72 A ATOM 2152 CEl PHE A 342 32.702 16.867 26.811 1.00 18.08 A ATOM 2153 CE2 PHE A 342 34.184 17.414 28.617 1.00 17.45 A ATOM 2154 CZ PHE A 342 33.790 17.578 27.298 1.00 16.56 A ATOM 2155 C PHE A 342 29.679 13.972 30.976 1.00 24.95 A ATOM 2156 O PHE A 342 30.002 12.798 30.777 1.00 23.95 A ATOM 2157 N GLU A 343 28.861 14.333 31.958 1.00 27.35 A ATOM 2158 CA GLU A 343 28.325 13.349 32.897 1.00 30.28 A ATOM 2159 CB GLU A 343 27.187 13.964 33.716 1.00 32.20 A ATOM 2160 CC GLU A 343 26.581 12.991 34.714 1.00 39.71 A ATOM 2161 CD GLU A 343 25.628 13.661 35.688 1.00 44.72 A ATOM 2162 OE1 GLU A 343 24.661 14.314 35.234 1.00 47.55 A ATOM 2163 0E2 GLU A 343 25.847 13.526 36.911 1.00 46.89 A ATOM 2164 C GLU A 343 27.852 12.017 32.305 1.00 28.98 A ATOM 2165 O GLU A 343 28.225 10.952 32.800 1.00 31.73 A ATOM 2166 N SER A 344 27.037 12.067 31.258 1.00 26.09 A ATOM 2167 CA SER A 344 26.520 10.838 30.656 1.00 28.36 A ATOM 2168 CB SER A 344 25.129 11.089 30.067 1.00 28.73 A ATOM 2169 OG SER A 344 25.203 11.942 28.940 1.00 30.91 A ATOM 2170 C SER A 344 27.407 10.214 29.577 1.00 27.66 A ATOM 2171 O SER A 344 26.987 9.281 28.900 1.00 28.66 A ATOM 2172 N VAL A 345 28.627 10.715 29.419 1.00 26.75 A ATOM 2173 CA VAL A 345 29.534 10.183 28.402 1.00 23.44 A ATOM 2174 CB VAL A 345 30.565 11.256 27.950 1.00 23.10 A ATOM 2175 CCI VAL A 345 31.589 10.631 26.995 1.00 22.24 A ATOM 2176 CO2 VAL A 345 29.854 12.418 27.275 1.00 20.05 A ATOM 2177 C VAL A 345 30.326 8.957 28.855 1.00 24.26 A ATOM 2178 O VAL A 345 30.876 8.930 29.960 1.00 22.83 A ATOM 2179 N THR A 346 30.374 7.942 27.997 1.00 21.77 A ATOM 2180 CA THR A 346 31.153 6.740 28.272 1.00 23.70 A ATOM 2181 CB THR A 346 30.391 5.455 27.857 1.00 26.53 A ATOM 2182 OG1 THR A 346 29.248 5.284 28.706 1.00 29.98 A ATOM 2183 CO2 THR A 346 31.289 4.231 27.990 1.00 24.28 A ATOM 2184 C THR A 346 32.383 6.945 27.385 1.00 23.43 A ATOM 2185 O THR A 346 32.306 6.827 26.160 1.00 24.50 A ATOM 2186 N TRP A 347 33.508 7.270 28.013 1.00 22.98 A ATOM 2187 CA TRP A 347 34.744 7.569 27.300 1.00 23.81 A ATOM 2188 CB TRP A 347 35.683 8.352 28.219 1.00 22.54 A ATOM 2189 CC TRP A 347 35.128 9.658 28.693 1.00 20.61 A ATOM 2190 CD2 TRP A 347 35.257 10.927 28.040 1.00 19.11 A ATOM 2191 CE2 TRP A 347 34.581 11.881 28.838 1.00 18.39 A ATOM 2192 CE3 TRP A 347 35.878 11.351 26.858 1.00 18.16 A ATOM 2193 CD1 TRP A 347 34.397 9.883 29.828 1.00 18.35 A ATOM 2194 NE1 TRP A 347 34.065 11.218 29.923 1.00 19.51 A ATOM 2195 CZ2 TRP A 347 34.510 13.234 28.491 1.00 16.88 A ATOM 2196 CZ3 TRP A 347 35.808 12.701 26.511 1.00 17.23 A ATOM 2197 CH2 TRP A 347 35.127 13.624 27.327 1.00 18.16 A ATOM 2198 C TRP A 347 35.538 6.429 26.675 1.00 25.79 A ATOM 2199 O TRP A 347 36.304 6.654 25.742 1.00 24.67 A ATOM 2200 N ALA A 348 35.360 5.215 27.183 1.00 27.10 A ATOM 2201 CA ALA A 348 36.116 4.063 26.697 1.00 27.46 A ATOM 2202 CB ALA A 348 35.899 2.869 27.636 1.00 27.09 A ATOM 2203 C ALA A 348 35.895 3.620 25.256 1.00 27.18 A ATOM 2204 O ALA A 348 36.830 3.148 24.613 1.00 29.41 A ATOM 2205 N ASN A 349 34.682 3.769 24.735 1.00 26.55 A ATOM 2206 CA ASN A 349 34.418 3.310 23.375 1.00 27.28 A ATOM 2207 CB ASN A 349 33.700 1.962 23.444 1.00 29.37 A ATOM 2208 CG ASN A 349 32.299 2.088 24.013 1.00 30.92 A ATOM 2209 ODi ASN A 349 32.045 2.942 24.859 1.00 30.17 A ATOM 2210 ND2 ASN A 349 31.386 1.237 23.553 1.00 33.52 A ATOM 2211 C ASN A 349 33.599 4.265 22.509 1.00 26.47 A ATOM 2212 O ASN A 349 32.669 3.843 21.819 1.00 25.87 A ATOM 2213 N LEU A 350 33.947 5.543 22.518 1.00 24.45 A ATOM 2214 CA LEU A 350 33.203 6.510 21.721 1.00 23.14 A ATOM 2215 CB LEU A 350 33.837 7.898 21.848 1.00 23.22 A ATOM 2216 CG LEU A 350 33.659 8.605 23.191 1.00 21.05 A ATOM 2217 CD1 LEU A 350 34.646 9.756 23.293 1.00 19.36 A ATOM 2218 CD2 LEU A 350 32.220 9.094 23.319 1.00 18.78 A ATOM 2219 C LEU A 350 33.082 6.152 20.240 1.00 22.60 A ATOM 2220 O LEU A 350 32.011 6.296 19.650 1.00 21.15 A ATOM 2221 N HIS A 351 34.165 5.689 19.627 1.00 23.13 A ATOM 2222 CA HIS A 351 34.089 5.387 18.204 1.00 27.83 A ATOM 2223 CB HIS A 351 35.506 5.325 17.596 1.00 29.36 A ATOM 2224 CG HIS A 351 36.082 3.950 17.493 1.00 32.07 A ATOM 2225 CD2 HIS A 351 36.611 3.128 18.431 1.00 32.39 A ATOM 2226 ND1 HIS A 351 36.197 3.285 16.291 1.00 33.02 A ATOM 2227 CEl HIS A 351 36.775 2.113 16.493 1.00 33.58 A ATOM 2228 NE2 HIS A 351 37.036 1.992 17.782 1.00 31.76 A ATOM 2229 C HIS A 351 33.258 4.144 17.874 1.00 28.12 A ATOM 2230 O HIS A 351 33.015 3.847 16.707 1.00 29.49 A ATOM 2231 N GLN A 352 32.800 3.442 18.908 1.00 29.28 A ATOM 2232 CA GLN A 352 31.963 2.255 18.726 1.00 29.67 A ATOM 2233 CB GLN 352 32.366 1.145 19.694 0.50 30.56 AC1 ATOM 2234 CG GLN 352 33.169 0.041 19.041 0.50 30.88 AC1 ATOM 2235 CD GLN 352 34.493 −0.186 19.729 0.50 31.21 AC1 ATOM 2236 OE1 GLN 352 34.541 −0.450 20.928 0.50 30.76 AC1 ATOM 2237 NE2 GLN 352 35.578 −0.084 18.971 0.50 32.30 AC1 ATOM 2238 C GLN A 352 30.504 2.638 18.963 1.00 30.42 A ATOM 2239 O GLN A 352 29.595 1.831 18.770 1.00 29.01 A ATOM 2240 N GLN A 353 30.290 3.875 19.397 1.00 27.64 A ATOM 2241 CA GLN A 353 28.948 4.365 19.652 1.00 27.42 A ATOM 2242 CB GLN A 353 28.977 5.401 20.775 1.00 25.77 A ATOM 2243 CG GLN A 353 29.408 4.837 22.115 1.00 27.34 A ATOM 2244 CD GLN A 353 29.638 5.914 23.156 1.00 27.19 A ATOM 2245 OE1 GLN A 353 28.875 6.872 23.252 1.00 28.29 A ATOM 2246 NE2 GLN A 353 30.687 5.753 23.951 1.00 28.79 A ATOM 2247 C GLN A 353 28.375 4.989 18.385 1.00 29.00 A ATOM 2248 O GLN A 353 29.118 5.455 17.516 1.00 29.14 A ATOM 2249 N THR A 354 27.053 4.984 18.276 1.00 27.31 A ATOM 2250 CA THR A 354 26.390 5.568 17.119 1.00 27.85 A ATOM 2251 CB THR A 354 24.991 4.941 16.904 1.00 30.69 A ATOM 2252 OG1 THR A 354 25.132 3.532 16.665 1.00 30.07 A ATOM 2253 CG2 THR A 354 24.289 5.585 15.709 1.00 29.58 A ATOM 2254 C THR A 354 26.244 7.062 17.376 1.00 26.85 A ATOM 2255 O THR A 354 25.592 7.475 18.329 1.00 25.77 A ATOM 2256 N PRO A 355 26.867 7.898 16.533 1.00 27.22 A ATOM 2257 CD PRO A 355 27.792 7.588 15.431 1.00 25.89 A ATOM 2258 CA PRO A 355 26.763 9.346 16.734 1.00 27.23 A ATOM 2259 CB PRO A 355 27.625 9.915 15.609 1.00 24.91 A ATOM 2260 CC PRO A 355 28.643 8.838 15.385 1.00 25.54 A ATOM 2261 C PRO A 355 25.322 9.837 16.641 1.00 28.07 A ATOM 2262 O PRO A 355 24.548 9.364 15.810 1.00 27.24 A ATOM 2263 N PRO A 356 24.941 10.792 17.500 1.00 28.28 A ATOM 2264 CD PRO A 356 25.752 11.560 18.462 1.00 28.31 A ATOM 2265 CA PRO A 356 23.572 11.306 17.448 1.00 28.44 A ATOM 2266 CB PRO A 356 23.539 12.301 18.604 1.00 28.11 A ATOM 2267 CC PRO A 356 24.946 12.832 18.612 1.00 26.86 A ATOM 2268 C PRO A 356 23.363 11.978 16.097 1.00 29.25 A ATOM 2269 O PRO A 356 24.304 12.537 15.529 1.00 27.27 A ATOM 2270 N ALA A 357 22.143 11.910 15.575 1.00 30.45 A ATOM 2271 CA ALA A 357 21.848 12.521 14.287 1.00 32.81 A ATOM 2272 CB ALA A 357 20.507 12.019 13.757 1.00 31.99 A ATOM 2273 C ALA A 357 21.824 14.035 14.448 1.00 35.05 A ATOM 2274 O ALA A 357 21.194 14.561 15.369 1.00 35.04 A ATOM 2275 N LEU A 358 22.516 14.730 13.552 1.00 37.81 A ATOM 2276 CA LEU A 358 22.578 16.185 13.597 1.00 42.15 A ATOM 2277 CB LEU A 358 23.679 16.681 12.658 1.00 39.54 A ATOM 2278 CC LEU A 358 25.086 16.285 13.109 1.00 39.51 A ATOM 2279 CD1 LEU A 358 26.102 16.686 12.062 1.00 39.29 A ATOM 2280 CD2 LEU A 358 25.395 16.953 14.445 1.00 40.01 A ATOM 2281 C LEU A 358 21.241 16.837 13.242 1.00 45.91 A ATOM 2282 O LEU A 358 20.874 16.927 12.069 1.00 45.71 A ATOM 2283 N THR A 359 20.530 17.290 14.275 1.00 50.06 A ATOM 2284 CA THR A 359 19.223 17.939 14.140 1.00 53.73 A ATOM 2285 CB THR A 359 19.353 19.428 13.726 1.00 54.04 A ATOM 2286 001 THR A 359 19.995 19.521 12.448 1.00 56.35 A ATOM 2287 CC2 THR A 359 20.158 20.204 14.763 1.00 54.32 A ATOM 2288 C THR A 359 18.309 17.236 13.139 1.00 54.47 A ATOM 2289 O THR A 359 18.483 16.016 12.930 1.00 55.90 A ATOM 2290 OXT THR A 359 17.407 17.908 12.595 1.00 56.97 A ATOM 2291 OH2 TIP S 1 42.566 19.118 34.302 1.00 15.09 S ATOM 2292 OH2 TIP S 2 41.052 32.378 19.857 1.00 15.82 S ATOM 2293 OH2 TIP S 3 37.014 33.030 17.747 1.00 16.95 S ATOM 2294 OH2 TIP S 5 45.353 24.370 18.152 1.00 16.85 S ATOM 2295 OH2 TIP S 6 31.896 13.930 33.235 1.00 20.42 S ATOM 2296 OH2 TIP S 7 50.351 22.781 28.249 1.00 21.14 S ATOM 2297 OH2 TIP S 8 45.246 −0.589 −0.734 1.00 17.74 S ATOM 2298 OH2 TIP S 11 46.249 −0.348 −8.523 1.00 21.32 S ATOM 2299 OH2 TIP S 14 45.756 11.148 29.680 1.00 21.94 S ATOM 2300 OH2 TIP S 15 44.273 13.157 34.592 1.00 15.61 S ATOM 2301 OH2 TIP S 17 53.598 3.722 −1.720 1.00 21.45 S ATOM 2302 OH2 TIP S 18 46.049 13.087 31.565 1.00 20.35 S ATOM 2303 OH2 TIP S 19 53.422 22.401 −3.280 1.00 23.26 S ATOM 2304 OH2 TIP S 20 34.587 7.922 5.383 1.00 22.58 S ATOM 2305 OH2 TIP S 21 45.053 27.379 19.376 1.00 29.60 S ATOM 2306 OH2 TIP S 23 28.899 36.416 28.633 1.00 31.68 S ATOM 2307 OH2 TIP S 24 35.531 11.645 −8.219 1.00 23.45 S ATOM 2308 OH2 TIP S 25 47.364 28.787 19.612 1.00 23.03 S ATOM 2309 OH2 TIP S 27 48.859 21.588 12.634 1.00 23.76 S ATOM 2310 OH2 TIP S 29 48.805 8.920 23.626 1.00 22.23 S ATOM 2311 OH2 TIP S 31 48.619 7.247 10.112 1.00 21.32 S ATOM 2312 OH2 TIP S 34 44.824 28.720 15.621 1.00 25.27 S ATOM 2313 OH2 TIP S 35 26.030 12.634 13.407 1.00 21.61 S ATOM 2314 OH2 TIP S 36 50.462 19.810 40.066 1.00 25.45 S ATOM 2315 OH2 TIP S 37 39.631 23.510 −0.239 1.00 30.88 S ATOM 2316 OH2 TIP S 40 44.734 42.655 10.346 1.00 30.84 S ATOM 2317 OH2 TIP S 41 54.653 3.902 1.503 1.00 27.14 S ATOM 2318 OH2 TIP S 45 45.693 21.923 39.754 1.00 28.30 S ATOM 2319 OH2 TIP S 47 47.820 16.413 7.805 1.00 25.73 S ATOM 2320 OH2 TIP S 48 50.292 31.412 29.642 1.00 32.79 S ATOM 2321 OH2 TIP S 49 26.056 16.646 34.827 1.00 29.80 S ATOM 2322 OH2 TIP S 52 31.714 10.996 31.855 1.00 29.15 S ATOM 2323 OH2 TIP S 53 46.108 23.843 −4.299 1.00 24.21 S ATOM 2324 OH2 TIP S 54 37.645 11.206 34.448 1.00 28.56 S ATOM 2325 OH2 TIP S 55 26.371 28.513 12.142 1.00 32.08 S ATOM 2326 OH2 TIP S 58 33.564 19.700 3.483 1.00 28.28 S ATOM 2327 OH2 TIP S 64 48.295 −0.632 14.280 1.00 32.13 S ATOM 2328 OH2 TIP S 65 40.064 26.036 34.324 1.00 24.17 S ATOM 2329 OH2 TIP S 66 29.570 3.958 14.729 1.00 28.94 S ATOM 2330 OH2 TIP S 72 60.085 11.604 6.814 1.00 38.35 S ATOM 2331 OH2 TIP S 73 39.203 44.403 18.686 1.00 26.61 S ATOM 2332 OH2 TIP S 76 47.312 12.366 27.366 1.00 28.51 S ATOM 2333 OH2 TIP S 80 43.862 33.771 33.329 1.00 28.82 S ATOM 2334 OH2 TIP S 81 57.890 13.106 2.128 1.00 40.62 S ATOM 2335 OH2 TIP S 82 41.663 34.381 32.043 1.00 19.35 S ATOM 2336 OH2 TIP S 85 50.974 40.331 19.200 1.00 21.14 S ATOM 2337 OH2 TIP S 88 47.925 −0.832 −6.556 1.00 24.11 S ATOM 2338 OH2 TIP S 90 27.231 28.336 33.481 1.00 27.64 S ATOM 2339 OH2 TIP S 91 43.651 −7.101 −7.995 1.00 24.33 S ATOM 2340 OH2 TIP S 92 49.325 4.387 19.370 1.00 28.02 S ATOM 2341 OH2 TIP S 93 46.231 11.549 33.898 1.00 29.40 S ATOM 2342 OH2 TIP S 94 63.889 24.831 1.168 1.00 26.53 S ATOM 2343 OH2 TIP S 96 56.396 4.952 −6.749 1.00 28.00 S ATOM 2344 OH2 TIP S 98 35.510 27.986 11.558 1.00 29.24 S ATOM 2345 OH2 TIP S 100 49.942 24.366 30.265 1.00 31.61 S ATOM 2346 OH2 TIP S 101 56.121 7.113 −8.298 1.00 31.57 S ATOM 2347 OH2 TIP S 102 58.318 19.957 −8.378 1.00 26.95 S ATOM 2348 OH2 TIP S 103 49.647 22.446 39.624 1.00 40.57 S ATOM 2349 OH2 TIP S 104 45.359 7.052 13.052 1.00 26.27 S ATOM 2350 OH2 TIP S 105 37.150 32.340 32.346 1.00 34.45 S ATOM 2351 OH2 TIP S 107 43.465 40.457 8.240 1.00 40.48 S ATOM 2352 OH2 TIP S 119 36.644 8.257 13.418 1.00 30.70 S ATOM 2353 OH2 TIP S 123 41.912 −8.974 −8.264 1.00 26.08 S ATOM 2354 OH2 TIP S 124 62.424 15.800 −7.411 1.00 24.08 S ATOM 2355 OH2 TIP S 126 37.266 18.656 −9.097 1.00 28.99 S ATOM 2356 OH2 TIP S 127 43.129 26.845 −14.606 1.00 25.19 S ATOM 2357 OH2 TIP S 128 36.339 32.639 29.802 1.00 29.25 S ATOM 2358 OH2 TIP S 130 54.051 14.561 26.498 1.00 33.93 S ATOM 2359 OH2 TIP S 131 41.805 −4.242 5.492 1.00 33.72 S ATOM 2360 OH2 TIP S 133 38.873 25.163 36.697 1.00 30.69 S ATOM 2361 OH2 TIP S 134 28.777 8.553 25.307 1.00 31.43 S ATOM 2362 OH2 TIP S 135 53.672 10.546 −12.803 1.00 33.45 S ATOM 2363 OH2 TIP S 136 59.892 15.434 11.467 1.00 31.39 S ATOM 2364 OH2 TIP S 137 31.040 12.361 35.470 1.00 34.07 S ATOM 2365 OH2 TIP S 139 33.489 14.292 −0.598 1.00 40.68 S ATOM 2366 OH2 TIP S 140 46.918 8.748 11.662 1.00 29.23 S ATOM 2367 OH2 TIP S 141 46.297 −7.287 −9.196 1.00 42.20 S ATOM 2368 OH2 TIP S 142 58.193 6.715 −4.685 1.00 35.48 S ATOM 2369 OH2 TIP S 143 44.598 4.435 12.503 1.00 27.68 S ATOM 2370 OH2 TIP S 144 27.003 5.999 12.450 1.00 36.30 S ATOM 2371 OH2 TIP S 145 43.676 32.852 35.735 1.00 35.70 S ATOM 2372 OH2 TIP S 146 35.783 18.628 36.452 1.00 34.62 S ATOM 2373 OH2 TIP S 147 25.402 4.058 20.638 1.00 45.03 S ATOM 2374 OH2 TIP S 148 45.839 35.853 33.724 1.00 35.47 S ATOM 2375 OH2 TIP S 149 22.176 18.976 16.752 1.00 31.87 S ATOM 2376 OH2 TIP S 150 43.986 33.179 10.162 1.00 37.70 S ATOM 2377 OH2 TIP S 151 50.653 20.347 42.428 1.00 35.80 S ATOM 2378 OH2 TIP S 152 47.843 24.314 9.506 1.00 31.05 S ATOM 2379 OH2 TIP S 153 44.693 5.273 −14.175 1.00 29.90 S ATOM 2380 OH2 TIP S 155 26.560 36.851 31.684 1.00 49.29 S ATOM 2381 OH2 TIP S 156 46.867 8.019 −12.951 1.00 29.21 S ATOM 2382 OH2 TIP S 157 30.432 28.741 12.438 1.00 37.76 S ATOM 2383 OH2 TIP S 158 41.004 20.553 6.423 1.00 39.53 S ATOM 2384 OH2 TIP S 159 49.258 20.069 29.294 1.00 33.97 S ATOM 2385 OH2 TIP S 160 48.082 28.459 16.489 1.00 33.10 S ATOM 2386 OH2 TIP S 161 47.448 18.625 27.683 1.00 34.87 S ATOM 2387 OH2 TIP S 162 19.687 20.632 23.411 1.00 35.01 S ATOM 2388 OH2 TIP S 163 32.402 −1.266 22.443 1.00 37.26 S ATOM 2389 OH2 TIP S 164 39.475 33.468 33.237 1.00 35.34 S ATOM 2390 OH2 TIP S 165 44.277 18.950 5.162 1.00 45.14 S ATOM 2391 OH2 TIP S 166 34.797 30.523 10.736 1.00 47.55 S ATOM 2392 OH2 TIP S 167 46.541 3.526 −14.949 1.00 26.54 S ATOM 2393 OH2 TIP S 168 36.333 16.371 1.539 1.00 38.68 S ATOM 2394 OH2 TIP S 169 46.761 38.936 27.403 1.00 34.66 S ATOM 2395 OH2 TIP S 170 24.163 13.264 11.375 1.00 41.23 S ATOM 2396 OH2 TIP S 171 48.459 15.018 31.951 1.00 38.11 S ATOM 2397 OH2 TIP S 172 34.261 23.193 40.004 1.00 48.96 S ATOM 2398 OH2 TIP S 173 45.924 −0.026 13.224 1.00 39.55 S ATOM 2399 OH2 TIP S 175 41.384 37.389 32.543 1.00 40.74 S ATOM 2400 OH2 TIP S 177 49.394 35.312 27.150 1.00 44.33 S ATOM 2401 OH2 TIP S 178 29.066 29.942 34.359 1.00 41.46 S ATOM 2402 OH2 TIP S 180 49.354 19.467 7.273 1.00 34.56 S ATOM 2403 OH2 TIP S 181 25.298 17.029 31.863 1.00 47.74 S ATOM 2404 OH2 TIP S 182 37.071 25.027 4.669 1.00 43.87 S ATOM 2405 OH2 TIP S 183 22.581 7.487 18.691 1.00 41.75 S ATOM 2406 OH2 TIP S 184 32.269 7.011 −1.891 1.00 48.84 S ATOM 2407 OH2 TIP S 185 48.234 0.494 6.833 1.00 48.16 S ATOM 2408 OH2 TIP S 187 20.008 14.658 19.211 1.00 45.27 S ATOM 2409 OH2 TIP S 188 49.341 22.698 42.272 1.00 42.20 S ATOM 2410 OH2 TIP S 190 61.292 18.260 −8.097 1.00 45.21 S ATOM 2411 OH2 TIP S 191 28.152 10.606 2.819 1.00 40.38 S ATOM 2412 OH2 TIP S 192 25.626 12.619 23.191 1.00 34.27 S ATOM 2413 OH2 TIP S 193 59.876 11.603 1.216 1.00 46.54 S ATOM 2414 OH2 TIP S 194 57.592 21.183 −10.646 1.00 45.82 S ATOM 2415 OH2 TIP S 195 31.509 36.649 21.499 1.00 38.73 S ATOM 2416 OH2 TIP S 197 50.270 −1.543 −6.136 1.00 42.66 S ATOM 2417 OH2 TIP S 198 24.467 8.729 13.088 1.00 42.78 S ATOM 2418 OH2 TIP S 199 38.098 8.699 25.759 1.00 32.80 S ATOM 2419 OH2 TIP S 200 57.831 11.358 −13.255 1.00 45.31 S ATOM 2420 OH2 TIP S 201 23.888 22.328 30.524 1.00 37.12 S ATOM 2421 OH2 TIP S 202 47.691 26.068 37.666 1.00 37.92 S ATOM 2422 OH2 TIP S 203 38.653 7.070 29.307 1.00 50.54 S ATOM 2423 OH2 TIP S 206 44.424 27.583 2.092 1.00 53.50 S ATOM 2424 OH2 TIP S 212 22.258 2.296 17.948 1.00 47.38 S ATOM 2425 OH2 TIP S 214 19.843 17.943 23.303 1.00 30.36 S ATOM 2426 OH2 TIP S 216 27.647 11.344 24.681 1.00 31.32 S ATOM 2427 OH2 TIP S 217 37.953 7.817 −9.284 1.00 45.97 S ATOM 2428 OH2 TIP S 218 33.845 34.040 12.124 1.00 38.11 S ATOM 2429 OH2 TIP S 219 58.484 15.269 13.717 1.00 38.26 S ATOM 2430 OH2 TIP S 220 48.526 40.920 26.583 1.00 35.23 S ATOM 2431 OH2 TIP S 222 52.094 21.184 38.122 1.00 29.86 S ATOM 2432 OH2 TIP S 223 36.889 5.881 3.281 1.00 37.63 S ATOM 2433 OH2 TIP S 224 47.642 −1.401 −10.684 1.00 34.89 S ATOM 2434 OH2 TIP S 226 47.284 2.916 19.133 1.00 34.10 S ATOM 2435 OH2 TIP S 227 42.468 4.463 −15.039 1.00 37.98 S ATOM 2436 OH2 TIP S 228 19.169 22.832 21.831 1.00 41.57 S ATOM 2437 OH2 TIP S 231 57.592 12.689 14.880 1.00 50.22 S ATOM 2438 OH2 TIP S 232 27.102 9.176 5.655 1.00 40.57 S ATOM 2439 OH2 TIP S 233 58.618 9.072 −11.925 1.00 50.71 S ATOM 2440 OH2 TIP S 234 22.822 25.342 19.945 1.00 34.93 S ATOM 2441 OH2 TIP S 236 24.831 32.218 28.901 1.00 37.69 S ATOM 2442 OH2 TIP S 237 20.045 10.774 16.992 1.00 39.57 S ATOM 2443 OH2 TIP S 238 58.019 19.850 15.679 1.00 41.42 S ATOM 2444 OH2 TIP S 239 19.490 20.949 26.114 1.00 34.55 S ATOM 2445 OH2 TIP S 240 61.187 26.377 7.346 1.00 39.68 S ATOM 2446 OH2 TIP S 241 33.680 38.342 19.389 1.00 48.93 S ATOM 2447 OH2 TIP S 242 51.539 31.612 10.881 1.00 55.65 S ATOM 2448 OH2 TIP S 244 25.872 14.431 30.404 1.00 46.69 S ATOM 2449 OH2 TIP S 248 37.332 5.849 9.544 1.00 43.81 S ATOM 2450 OH2 TIP S 250 39.087 −1.293 −9.655 1.00 42.96 S ATOM 2451 OH2 TIP S 258 23.938 30.000 30.010 1.00 38.89 S ATOM 2452 OH2 TIP S 259 24.949 29.749 32.578 1.00 40.17 S ATOM 2453 OH2 TIP S 260 32.111 17.986 1.918 1.00 48.36 S ATOM 2454 OH2 TIP S 266 21.404 12.876 25.603 1.00 57.17 S ATOM 2455 OH2 TIP S 269 35.425 36.767 12.550 1.00 30.70 S ATOM 2456 OH2 TIP S 270 52.438 25.529 30.131 1.00 44.85 S ATOM 2457 OH2 TIP S 271 53.299 20.156 36.003 1.00 37.15 S ATOM 2458 OH2 TIP S 272 50.914 6.919 23.723 1.00 43.29 S ATOM 2459 OH2 TIP S 274 31.578 30.795 11.014 1.00 50.15 S ATOM 2460 OH2 TIP S 275 26.341 7.243 22.447 1.00 39.40 S ATOM 2461 OH2 TIP S 276 60.392 18.195 10.235 1.00 37.91 S ATOM 2462 OH2 TIP S 277 47.355 −9.081 −10.821 1.00 48.18 S ATOM 2463 OH2 TIP S 279 41.304 6.175 −16.647 1.00 38.12 S ATOM 2464 OH2 TIP S 282 33.299 21.620 37.881 1.00 46.29 S ATOM 2465 OH2 TIP S 283 56.469 26.112 −8.575 1.00 43.71 S ATOM 2466 OH2 TIP S 287 48.382 26.573 7.246 1.00 41.43 S ATOM 2467 OH2 TIP S 288 56.240 7.245 −11.331 1.00 41.79 S ATOM 2468 OH2 TIP S 290 49.060 14.978 28.166 1.00 37.03 S ATOM 2469 OH2 TIP S 291 37.095 44.270 26.442 1.00 45.08 S ATOM 2470 OH2 TIP S 292 47.814 −0.384 −13.299 1.00 48.60 S ATOM 2471 OH2 TIP S 297 58.081 2.784 −7.841 1.00 41.89 S ATOM 2472 OH2 TIP S 298 36.447 45.321 18.644 1.00 54.91 S ATOM 2473 OH2 TIP S 299 49.029 23.328 1.767 1.00 30.55 S ATOM 2474 OH2 TIP S 301 24.375 13.771 8.634 1.00 48.47 S ATOM 2475 OH2 TIP S 303 47.904 36.798 28.653 1.00 35.76 S ATOM 2476 OH2 TIP S 305 51.156 40.821 27.172 1.00 43.59 S ATOM 2477 OH2 TIP S 306 32.943 28.917 35.227 1.00 42.60 S ATOM 2478 OH2 TIP S 307 58.462 28.373 6.251 1.00 46.15 S ATOM 2479 OH2 TIP S 308 41.964 30.940 36.712 1.00 48.26 S ATOM 2480 OH2 TIP S 313 51.176 −1.922 −3.336 1.00 50.61 S ATOM 2481 OH2 TIP S 1001 21.319 36.868 23.805 1.00 36.97 S ATOM 2482 OH2 TIP S 1002 48.880 32.620 27.617 1.00 44.40 S ATOM 2483 OH2 TIP S 1003 61.880 19.473 11.767 1.00 45.49 S ATOM 2484 OH2 TIP S 1004 52.770 21.424 26.815 1.00 24.43 S ATOM 2485 OH2 TIP S 1005 35.373 29.094 36.197 1.00 35.97 S ATOM 2486 OH2 TIP S 1006 40.815 −6.636 4.389 1.00 43.15 S ATOM 2487 OH2 TIP S 1007 44.953 1.286 11.272 1.00 49.45 S ATOM 2488 OH2 TIP S 1010 21.004 16.168 27.009 1.00 48.51 S ATOM 2489 OH2 TIP S 1011 47.094 41.786 9.243 1.00 50.10 S ATOM 2490 OH2 TIP S 1012 32.479 2.978 14.158 1.00 49.47 S ATOM 2491 O12 GLC G 1 48.557 11.372 −12.279 1.00 40.72 G ATOM 2492 C11 GLC G 1 48.836 12.133 −11.097 1.00 38.05 G ATOM 2493 C13 GLC G 1 49.266 13.554 −11.476 1.00 38.09 G ATOM 2494 O14 GLC G 1 49.559 14.299 −10.292 1.00 33.99 G ATOM 2495 C15 GLC G 1 48.150 14.257 −12.257 1.00 37.32 G ATOM 2496 O16 GLC G 1 48.574 15.582 −12.604 1.00 36.74 G ATOM 2497 O12 GLC G 2 40.114 −6.634 −6.562 1.00 33.52 G ATOM 2498 C11 GLC G 2 38.967 −6.592 −7.404 1.00 31.05 G ATOM 2499 C13 GLC G 2 37.712 −6.417 −6.552 1.00 31.56 G ATOM 2500 O14 GLC G 2 36.554 −6.406 −7.389 1.00 30.70 G ATOM 2501 C1S GLC G 2 37.792 −5.109 −5.761 1.00 30.03 G ATOM 2502 O16 GLC G 2 36.609 −4.961 −4.975 1.00 29.66 G ATOM 2503 O12 GLC G 3 44.030 8.243 −13.470 1.00 37.90 G ATOM 2504 C11 GLC G 3 43.950 9.648 −13.690 1.00 38.47 G ATOM 2505 C13 GLC G 3 42.747 9.974 −14.579 1.00 39.52 G ATOM 2506 O14 GLC G 3 41.551 9.526 −13.942 1.00 39.39 G ATOM 2507 C15 GLC G 3 42.878 9.280 −15.934 1.00 41.43 G ATOM 2508 O16 GLC G 3 41.736 9.613 −16.731 1.00 40.78 G ATOM 2509 O12 GLC G S 40.556 1.005 2.289 1.00 45.25 G ATOM 2510 C11 GLC G S 40.966 2.332 1.960 1.00 40.56 G ATOM 2511 C13 GLC G S 40.187 3.327 2.814 1.00 40.36 G ATOM 2512 O14 GLC G S 38.791 3.169 2.572 1.00 40.71 G ATOM 2513 CiS GLC G S 40.619 4.751 2.464 1.00 40.04 G ATOM 2514 O16 GLC G S 39.885 5.681 3.256 1.00 36.89 G ATOM 2515 O12 GLC G 6 36.951 22.702 40.046 1.00 63.04 G ATOM 2516 C11 GLC G 6 37.592 21.583 39.422 1.00 62.46 G ATOM 2517 C13 GLC G 6 38.104 21.978 38.030 1.00 61.14 G ATOM 2518 O14 GLC G 6 39.034 23.054 38.168 1.00 61.72 G ATOM 2519 C15 GLC G 6 36.948 22.429 37.126 1.00 60.51 G ATOM 2520 O16 GLC G 6 35.992 21.372 36.960 1.00 58.61 G ATOM 2521 O12 GLC G 7 37.316 0.281 14.299 1.00 73.45 G ATOM 2522 C11 GLC G 7 37.655 −0.758 15.222 1.00 72.78 G ATOM 2523 C13 GLC G 7 36.592 −1.856 15.157 1.00 72.98 G ATOM 2524 014 GLC G 7 35.320 −1.299 15.498 1.00 73.88 G ATOM 2525 C15 GLC G 7 36.924 −2.989 16.134 1.00 73.66 G ATOM 2526 O16 GLC G 7 36.972 −2.493 17.478 1.00 75.38 G ATOM 2527 O12 GLC G 8 51.921 21.898 5.908 1.00 62.51 G ATOM 2528 C11 GLC G 8 52.447 20.871 5.063 1.00 63.42 G ATOM 2529 C13 GLC G 8 51.476 20.597 3.908 1.00 64.28 G ATOM 2530 O14 GLC G 8 51.297 21.794 3.150 1.00 66.28 G ATOM 2531 C15 GLC G 8 50.121 20.137 4.448 1.00 64.49 G ATOM 2532 O16 GLC G 8 49.233 19.886 3.357 1.00 64.01 G ATOM 2533 O12 GLC G 10 36.044 37.499 29.523 1.00 56.89 G ATOM 2534 C11 GLC G 10 35.164 36.645 30.259 1.00 56.97 G ATOM 2535 C13 GLC G 10 33.849 36.489 29.494 1.00 56.11 G ATOM 2536 O14 GLC G 10 33.248 37.772 29.308 1.00 56.44 G ATOM 2537 C15 GLC G 10 32.900 35.580 30.277 1.00 55.84 G ATOM 2538 O16 GLC G 10 31.674 35.442 29.557 1.00 55.39 G ATOM 2539 O3G ATP N 1 46.280 25.658 5.170 1.00 51.49 N ATOM 2540 PG ATP N 1 46.464 25.053 3.691 1.00 52.22 N ATOM 2541 O1G ATP N 1 47.406 23.911 3.763 1.00 51.41 N ATOM 2542 O2G ATP N 1 46.794 26.182 2.784 1.00 52.07 N ATOM 2543 O3B ATP N 1 44.976 24.513 3.344 1.00 51.01 N ATOM 2544 PB ATP N 1 44.560 22.969 3.605 1.00 50.20 N ATOM 2545 O1B ATP N 1 43.083 22.898 3.669 1.00 49.41 N ATOM 2546 O2B ATP N 1 45.345 22.474 4.766 1.00 50.34 N ATOM 2547 O3A ATP N 1 45.070 22.231 2.255 1.00 47.77 N ATOM 2548 PA ATP N 1 45.075 20.613 2.121 1.00 42.84 N ATOM 2549 O1A ATP N 1 45.547 20.291 0.754 1.00 43.81 N ATOM 2550 O2A ATP N 1 45.807 20.035 3.270 1.00 45.03 N ATOM 2551 O5* ATP N 1 43.516 20.223 2.245 1.00 41.73 N ATOM 2552 C5* ATP N 1 42.528 20.925 1.489 1.00 37.57 N ATOM 2553 C4* ATP N 1 41.127 20.379 1.776 1.00 39.45 N ATOM 2554 O4* ATP N 1 40.907 19.024 1.279 1.00 37.72 N ATOM 2555 C3* ATP N 1 40.777 20.321 3.251 1.00 38.48 N ATOM 2556 O3* ATP N 1 40.360 21.615 3.697 1.00 40.42 N ATOM 2557 C2* ATP N 1 39.608 19.374 3.270 1.00 37.58 N ATOM 2558 O2* ATP N 1 38.410 20.076 2.924 1.00 35.98 N ATOM 2559 C1* ATP N 1 39.939 18.346 2.173 1.00 35.55 N ATOM 2560 N9 ATP N 1 40.628 17.1S6 2.747 1.00 31.76 N ATOM 2561 C8 ATP N 1 41.864 17.126 3.274 1.00 30.49 N ATOM 2562 N7 ATP N 1 42.143 15.877 3.667 1.00 29.7S N ATOM 2563 C5 ATP N 1 41.088 15.118 3.390 1.00 27.49 N ATOM 2564 C4 ATP N 1 40.125 15.92S 2.810 1.00 30.02 N ATOM 2565 N3 ATP N 1 38.937 15.389 2.431 1.00 27.11 N ATOM 2566 C2 ATP N 1 38.679 14.085 2.615 1.00 25.62 N ATOM 2567 N1 ATP N 1 39.S97 13.283 3.175 1.00 21.76 N ATOM 2568 C6 ATP N 1 40.800 13.768 3.571 1.00 23.90 N ATOM 2569 N6 ATP N 1 41.698 12.964 4.127 1.00 21.94 N ATOM 2570 S SO4 I 1 58.680 8.493 −0.639 1.00 56.05 I ATOM 2571 O1 SO4 I 1 57.956 7.875 0.483 1.00 58.83 I ATOM 2572 O2 SO4 I 1 57.886 9.607 −1.188 1.00 57.04 I ATOM 2573 O3 SO4 I 1 58.906 7.478 −1.683 1.00 57.47 I ATOM 2574 O4 SO4 I 1 59.976 9.008 −0.156 1.00 57.S1 I ATOM 2575 S SO4 I 2 39.339 4.855 7.087 1.00 84.24 I ATOM 2576 O1 SO4 I 2 39.390 6.175 7.711 1.00 84.02 I ATOM 2577 O2 SO4 I 2 40.101 4.897 5.797 1.00 84.7S I ATOM 2578 O3 SO4 I 2 37.936 4.506 6.766 1.00 84.94 I ATOM 2579 O4 SO4 I 2 39.931 3.842 7.9S4 1.00 84.44 I ATOM 2580 S SO4 I 3 38.987 −2.256 3.310 1.00 58.58 I ATOM 2581 O1 SO4 I 3 37.734 −1.675 3.827 1.00 59.11 I ATOM 2582 O2 SO4 I 3 39.460 −1.4S4 2.172 1.00 59.91 I ATOM 2583 O3 SO4 I 3 38.743 −3.640 2.866 1.00 50.97 I ATOM 2584 O4 SO4 I 3 40.014 −2.260 4.369 1.00 59.S8 I ATOM 2585 S SO4 I 4 34.397 5.289 30.981 1.00 64.34 I ATOM 2586 O1 SO4 I 4 33.627 6.528 30.742 1.00 60.43 I ATOM 2587 O2 SO4 I 4 34.337 4.427 29.782 1.00 60.11 I ATOM 2588 O3 SO4 I 4 33.816 4.572 32.133 1.00 64.39 I ATOM 2589 O4 SO4 I 4 35.806 S.626 31.277 1.00 63.SS I ATOM 2590 S SO4 I S 55.074 −6.984 −3.711 1.00 75.40 I ATOM 2591 O1 SO4 I S 54.657 −7.S18 −2.399 1.00 74.66 I ATOM 2592 O2 SO4 I S 54.209 −5.84S −4.06S 1.00 74.96 I ATOM 2593 O3 SO4 I S 54.9S0 −8.034 −4.742 1.00 74.22 I ATOM 2594 O4 SO4 I S 56.477 −6.532 −3.633 1.00 7S.1S I ATOM 2595 O2 PO4 P 100 57.362 24.998 13.149 1.00 66.76 P ATOM 2596 O3 PO4 P 100 59.399 26.166 13.761 1.00 66.89 P ATOM 2597 O4 PO4 P 100 57.761 25.606 1S.462 1.00 67.43 P ATOM 2598 O1 PO4 P 100 57.264 27.325 13.818 1.00 6S.91 P ATOM 2599 P PO4 P 100 57.947 26.025 14.048 1.00 66.69 P ATOM 2600 CB GLU 80 50.411 3.97S −13.538 0.50 23.31 AC2 ATOM 2601 CG GLU 80 51.306 4.896 −14.362 0.50 24.09 AC2 ATOM 2602 CD GLU 80 52.180 5.798 −13.409 0.50 2S.31 AC2 ATOM 2603 OE1 GLU 80 52.841 5.289 −12.580 0.50 22.80 AC2 ATOM 2604 OE2 GLU 80 52.212 7.018 −13.774 0.50 28.07 AC2 ATOM 260S CB SER 105 37.582 −1.281 −6.192 0.502 1.16 AC2 ATOM 2606 OG SER 105 37.127 −1.871 −4.988 0.502 0.42 AC2 ATOM 2607 CB ARG 116 59.520 22.977 −7.867 0.503 1.00 AC2 ATOM 2608 CG ARG 116 60.312 24.192 −8.323 0.503 2.50 AC2 ATOM 2609 CD ARC 116 60.266 24.349 −9.838 0.503 4.11 AC2 ATOM 2610 NE ARC 116 61.045 25.499 −10.290 0.50 36.67 AC2 ATOM 2611 CZ ARC 116 60.729 26.766 −10.035 0.50 37.26 AC2 ATOM 2612 NH1 ARC 116 59.642 27.053 −9.331 0.50 38.99 AC2 ATOM 2613 NH2 ARC 116 61.503 27.746 −10.479 0.50 37.83 AC2 ATOM 2614 CB LEU 145 49.693 8.642 6.631 0.50 15.29 AC2 ATOM 2615 CC LEU 145 50.783 8.664 5.552 0.50 14.29 AC2 ATOM 2616 CD1 LEU 145 50.264 9.373 4.305 0.50 8.20 AC2 ATOM 2617 CD2 LEU 145 52.030 9.361 6.087 0.50 10.66 AC2 ATOM 2618 CB ARC 183 27.455 16.155 24.989 0.50 19.21 AC2 ATOM 2619 CC ARC 183 28.077 15.397 26.147 0.50 18.46 AC2 ATOM 2620 CD ARC 183 27.002 14.945 27.127 0.50 19.72 AC2 ATOM 2621 NE ARC 183 26.016 14.086 26.478 0.50 18.79 AC2 ATOM 2622 CZ ARC 183 24.703 14.279 26.539 0.50 18.52 AC2 ATOM 2623 NH1 ARC 183 24.213 15.305 27.221 0.50 15.35 AC2 ATOM 2624 NH2 ARC 183 23.881 13.445 25.915 0.50 17.55 AC2 ATOM 2625 CB SER 191 38.479 10.847 23.036 0.50 16.57 AC2 ATOM 2626 OC SER 191 37.418 10.765 23.973 0.50 18.62 AC2 ATOM 2627 CB CLU 209 38.645 24.079 8.551 0.50 22.02 AC2 ATOM 2628 CC CLU 209 37.769 25.296 8.263 0.50 23.40 AC2 ATOM 2629 CD CLU 209 37.513 26.175 9.483 0.50 24.27 AC2 ATOM 2630 OE1 CLU 209 37.076 27.328 9.288 0.50 25.25 AC2 ATOM 2631 OE2 CLU 209 37.737 25.727 10.629 0.50 20.24 AC2 ATOM 2632 CB CLN 247 38.598 32.546 14.790 0.50 18.71 AC2 ATOM 2633 CC CLN 247 38.077 33.665 13.900 0.50 16.95 AC2 ATOM 2634 CD CLN 247 38.614 33.598 12.479 0.50 19.13 AC2 ATOM 2635 OE1 CLN 247 39.763 33.221 12.246 0.50 17.24 AC2 ATOM 2636 NE2 CLN 247 37.780 33.979 11.520 0.50 19.88 AC2 ATOM 2637 CE LYS 315 34.978 25.150 36.369 0.50 20.49 AC2 ATOM 2638 NZ LYS 315 34.183 24.074 37.023 0.50 17.05 AC2 ATOM 2639 CB CLN 352 32.365 1.170 19.731 0.50 31.10 AC2 ATOM 2640 CC CLN 352 33.833 0.778 19.683 0.50 32.11 AC2 ATOM 2641 CD CLN 352 34.190 0.027 18.419 0.50 33.04 AC2 ATOM 2642 OE1 CLN 352 33.906 0.485 17.314 0.50 34.87 AC2 ATOM 2643 NE2 CLN 352 34.819 −1.133 18.575 0.50 32.08 AC2

Example 3 Co-Ordinates for the PDK1 Fragment without Alternate Side Chains

REMARK coordinates from restrained individual B-factor refinement REMARK refinement resolution: 25.0-2.0 A REMARK starting r = 0.1972 free_r = 0.2220 REMARK final r = 0.1954 free_r = 0.2224 REMARK B rmsd for bonded mainchain atoms = 1.501 target = 1.5 REMARK B rmsd for bonded sidechain atoms = 2.235 target = 2.0 REMARK B rmsd for angle mainchain atoms = 2.347 target = 2.0 REMARK B rmsd for angle sidechain atoms = 3.302 target = 2.5 REMARK rweight = 0.0900 (with wa = 1.29263) REMARK target = mlf steps = 30 REMARK sg = P3(2)21 a = 123.013 b = 123.013 c = 47.624 alpha = 90 beta = 90 gamma = 120 REMARK parameter file 1: /dd1/david/projects/PDK1_new/CNS/prot.par REMARK parameter file 2: /dd1/david/projects/PDK1_new/CNS/atp.par REMARK parameter file 3: CNS_TOPPAR:water_rep.param REMARK parameter file 4: CNS_TOPPAR:ion.param REMARK parameter file 5: /dd1/david/projects/PDK1_new/CNS/glycerol.par REMARK molecular structure file: ../generate/alternate.mtf REMARK input coordinates: ../minimize/minimize.pdb REMARK reflection file = ../../1/hkl/cns.hkl REMARK ncs = none REMARK B-correction resolution: 6.0-2.0 REMARK initial B-factor correction applied to fobs: REMARK B11 = −2.766 B22 = −2.766 B33 = 5.532 REMARK B12 = −0.375 B13 =   0.000 B23 = 0.000 REMARK B-factor correction applied to coordinate array B: 0.031 REMARK bulk solvent: density level = 0.378441 e/A{circumflex over ( )}3, B-factor = 52.6885 A{circumflex over ( )}2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with |Fobs| > 10000 * rms(Fobs) rejected REMARK theoretical total number of refl. in resol. range: 28210 ( 100.0% ) REMARK number of unobserved reflections (no entry or |F| = 0): 568 (  2.0% ) REMARK number of reflections rejected: 0 (  0.0% ) REMARK total number of reflections used: 27642 (  98.0% ) REMARK number of reflections in working set: 27063 (  95.9% ) REMARK number of reflections in test set: 579 (  2.1% ) CRYST1 123.013 123.013 47.624 90.00 90.00 120.00 P 32 2 1 REMARK FILENAME = “bindividual.pdb” REMARK DATE: 16-Apr-2002 18:31:12   created by user: david REMARK VERSION: 1.0 ATOM 1 CB PRO A 71 58.912 −7.251 8.216 1.00 67.78 A ATOM 2 CG PRO A 71 59.621 −6.941 9.534 1.00 69.16 A ATOM 3 C PRO A 71 59.493 −6.506 5.894 1.00 67.06 A ATOM 4 O PRO A 71 59.196 −5.318 5.766 1.00 66.66 A ATOM 5 N PRO A 71 60.984 −6.073 7.833 1.00 67.86 A ATOM 6 CD PRO A 71 60.554 −5.762 9.207 1.00 68.24 A ATOM 7 CA PRO A 71 60.040 −7.035 7.217 1.00 67.75 A ATOM 8 N PRO A 72 59.356 −7.385 4.890 1.00 66.32 A ATOM 9 CD PRO A 72 59.712 −8.816 4.898 1.00 67.17 A ATOM 10 CA PRO A 72 58.840 −6.986 3.578 1.00 65.61 A ATOM 11 CB PRO A 72 58.672 −8.321 2.858 1.00 66.47 A ATOM 12 CG PRO A 72 59.796 −9.133 3.419 1.00 67.57 A ATOM 13 C PRO A 72 57.527 −6.208 3.673 1.00 63.94 A ATOM 14 O PRO A 72 56.710 −6.451 4.561 1.00 64.11 A ATOM 15 N ALA A 73 57.341 −5.268 2.753 1.00 61.57 A ATOM 16 CA ALA A 73 56.133 −4.454 2.708 1.00 58.74 A ATOM 17 CB ALA A 73 56.438 −3.030 3.165 1.00 58.05 A ATOM 18 C ALA A 73 55.626 −4.448 1.271 1.00 56.78 A ATOM 19 O ALA A 73 56.347 −4.834 0.349 1.00 56.95 A ATOM 20 N PRO A 74 54.372 −4.024 1.057 1.00 54.15 A ATOM 21 CD PRO A 74 53.335 −3.610 2.018 1.00 53.31 A ATOM 22 CA PRO A 74 53.856 −4.003 −0.314 1.00 52.54 A ATOM 23 CB PRO A 74 52.474 −3.375 −0.148 1.00 52.86 A ATOM 24 CG PRO A 74 52.067 −3.824 1.226 1.00 52.88 A ATOM 25 C PRO A 74 54.772 −3.167 −1.204 1.00 50.08 A ATOM 26 O PRO A 74 55.559 −2.361 −0.708 1.00 49.96 A ATOM 27 N ALA A 75 54.680 −3.366 −2.514 1.00 47.58 A ATOM 28 CA ALA A 75 55.503 −2.602 −3.446 1.00 44.69 A ATOM 29 CB ALA A 75 55.312 −3.121 −4.870 1.00 46.14 A ATOM 30 C ALA A 75 55.100 −1.134 −3.371 1.00 41.55 A ATOM 31 O ALA A 75 53.947 −0.813 −3.086 1.00 41.01 A ATOM 32 N LYS A 76 56.053 −0.245 −3.619 1.00 38.31 A ATOM 33 CA LYS A 76 55.781 1.184 −3.588 1.00 35.72 A ATOM 34 CB LYS A 76 57.053 1.957 −3.930 1.00 37.70 A ATOM 35 CG LYS A 76 57.123 3.356 −3.350 1.00 40.99 A ATOM 36 CD LYS A 76 57.262 3.316 −1.836 1.00 40.04 A ATOM 37 CE LYS A 76 57.511 4.705 −1.277 1.00 42.08 A ATOM 38 NZ LYS A 76 57.681 4.695 0.202 1.00 42.99 A ATOM 39 C LYS A 76 54.708 1.467 −4.638 1.00 32.65 A ATOM 40 O LYS A 76 54.814 1.005 −5.770 1.00 31.41 A ATOM 41 N LYS A 77 53.668 2.207 −4.270 1.00 28.59 A ATOM 42 CA LYS A 77 52.619 2.517 −5.232 1.00 25.72 A ATOM 43 CB LYS A 77 51.316 2.865 −4.509 1.00 26.22 A ATOM 44 CG LYS A 77 50.796 1.731 −3.631 1.00 27.15 A ATOM 45 CD LYS A 77 49.487 2.089 −2.967 1.00 26.80 A ATOM 46 CE LYS A 77 49.136 1.091 −1.870 1.00 27.31 A ATOM 47 NZ LYS A 77 48.998 −0.296 −2.380 1.00 27.17 A ATOM 48 C LYS A 77 53.053 3.668 −6.137 1.00 24.67 A ATOM 49 O LYS A 77 54.010 4.377 −5.829 1.00 21.60 A ATOM 50 N ARG A 78 52.351 3.838 −7.254 1.00 23.66 A ATOM 51 CA ARG A 78 52.662 4.897 −8.211 1.00 26.14 A ATOM 52 CB ARG A 78 53.574 4.344 −9.318 1.00 28.57 A ATOM 53 CG ARG A 78 53.017 3.139 −10.050 1.00 34.78 A ATOM 54 CD ARG A 78 54.092 2.465 −10.896 1.00 40.96 A ATOM 55 NE ARG A 78 53.560 1.364 −11.700 1.00 48.93 A ATOM 56 CZ ARG A 78 52.985 0.270 −11.203 1.00 52.58 A ATOM 57 NH1 ARG A 78 52.860 0.113 −9.889 1.00 54.60 A ATOM 58 NH2 ARG A 78 52.530 −0.672 −12.022 1.00 54.09 A ATOM 59 C ARG A 78 51.382 5.488 −8.803 1.00 23.76 A ATOM 60 O ARG A 78 50.311 4.888 −8.706 1.00 24.25 A ATOM 61 N PRO A 79 51.475 6.676 −9.428 1.00 21.76 A ATOM 62 CD PRO A 79 52.691 7.475 −9.668 1.00 20.82 A ATOM 63 CA PRO A 79 50.301 7.325 −10.021 1.00 21.96 A ATOM 64 CB PRO A 79 50.910 8.481 −10.816 1.00 22.27 A ATOM 65 CG PRO A 79 52.124 8.831 −10.014 1.00 22.12 A ATOM 66 C PRO A 79 49.446 6.413 −10.903 1.00 22.86 A ATOM 67 O PRO A 79 48.213 6.461 −10.842 1.00 20.52 A ATOM 68 N GLU A 80 50.103 5.586 −11.714 1.00 21.87 A ATOM 69 CA GLU A 80 49.403 4.685 −12.628 1.00 22.99 A ATOM 70 CB GLU A 80 50.393 3.994 −13.571 1.00 25.24 A ATOM 71 CG GLU A 80 51.230 2.907 −12.925 1.00 28.75 A ATOM 72 CD GLU A 80 52.157 2.224 −13.913 1.00 31.99 A ATOM 73 OE1 GLU A 80 53.072 2.897 −14.433 1.00 34.34 A ATOM 74 OE2 GLU A 80 51.969 1.015 −14.172 1.00 32.83 A ATOM 75 C GLU A 80 48.556 3.631 −11.912 1.00 22.09 A ATOM 76 O GLU A 80 47.692 3.013 −12.530 1.00 22.37 A ATOM 77 N ASP A 81 48.804 3.413 −10.622 1.00 19.97 A ATOM 78 CA ASP A 81 48.026 2.423 −9.874 1.00 19.93 A ATOM 79 CB ASP A 81 48.736 2.029 −8.571 1.00 21.19 A ATOM 80 CG ASP A 81 50.089 1.380 −8.807 1.00 22.46 A ATOM 81 OD1 ASP A 81 50.195 0.554 −9.731 1.00 24.22 A ATOM 82 OD2 ASP A 81 51.043 1.685 −8.058 1.00 23.33 A ATOM 83 C ASP A 81 46.652 2.975 −9.518 1.00 20.85 A ATOM 84 O ASP A 81 45.793 2.246 −9.015 1.00 19.96 A ATOM 85 N PHE A 82 46.445 4.258 −9.804 1.00 18.91 A ATOM 86 CA PHE A 82 45.200 4.934 −9.465 1.00 19.30 A ATOM 87 CB PHE A 82 45.475 6.027 −8.427 1.00 18.43 A ATOM 88 CG PHE A 82 46.134 5.531 −7.175 1.00 18.01 A ATOM 89 CD1 PHE A 82 45.371 5.136 −6.084 1.00 17.19 A ATOM 90 CD2 PHE A 82 47.520 5.460 −7.086 1.00 18.99 A ATOM 91 CE1 PHE A 82 45.977 4.676 −4.918 1.00 17.12 A ATOM 92 CE2 PHE A 82 48.137 5.000 −5.925 1.00 19.64 A ATOM 93 CZ PHE A 82 47.361 4.607 −4.838 1.00 18.00 A ATOM 94 C PHE A 82 44.476 5.596 −10.621 1.00 20.81 A ATOM 95 O PHE A 82 45.066 5.933 −11.649 1.00 20.34 A ATOM 96 N LYS A 83 43.182 5.792 −10.411 1.00 19.80 A ATOM 97 CA LYS A 83 42.321 6.478 −11.353 1.00 21.65 A ATOM 98 CB LYS A 83 41.096 5.625 −11.687 1.00 22.02 A ATOM 99 CG LYS A 83 40.062 6.326 −12.550 1.00 28.93 A ATOM 100 CD LYS A 83 38.974 5.355 −12.981 1.00 34.20 A ATOM 101 CE LYS A 83 37.909 6.042 −13.824 1.00 38.10 A ATOM 102 NZ LYS A 83 37.179 7.086 −13.043 1.00 43.33 A ATOM 103 C LYS A 83 41.913 7.702 −10.541 1.00 20.74 A ATOM 104 O LYS A 83 41.084 7.606 −9.635 1.00 20.98 A ATOM 105 N PHE A 84 42.513 8.848 −10.835 1.00 19.99 A ATOM 106 CA PHE A 84 42.188 10.049 −10.083 1.00 18.63 A ATOM 107 CB PHE A 84 43.279 11.103 −10.258 1.00 18.95 A ATOM 108 CG PHE A 84 44.571 10.741 −9.587 1.00 17.68 A ATOM 109 CD1 PHE A 84 45.498 9.926 −10.224 1.00 18.16 A ATOM 110 CD2 PHE A 84 44.843 11.183 −8.299 1.00 19.66 A ATOM 111 CE1 PHE A 84 46.676 9.556 −9.589 1.00 18.09 A ATOM 112 CE2 PHE A 84 46.021 10.816 −7.653 1.00 18.89 A ATOM 113 CZ PHE A 84 46.936 10.002 −8.301 1.00 17.33 A ATOM 114 C PHE A 84 40.834 10.617 −10.460 1.00 19.69 A ATOM 115 O PHE A 84 40.391 10.489 −11.601 1.00 20.72 A ATOM 116 N GLY A 85 40.178 11.233 −9.484 1.00 16.80 A ATOM 117 CA GLY A 85 38.872 11.810 −9.716 1.00 17.73 A ATOM 118 C GLY A 85 38.819 13.280 −9.346 1.00 18.75 A ATOM 119 O GLY A 85 39.740 14.043 −9.650 1.00 18.45 A ATOM 120 N LYS A 86 37.753 13.673 −8.659 1.00 16.00 A ATOM 121 CA LYS A 86 37.571 15.064 −8.278 1.00 18.26 A ATOM 122 CB LYS A 86 36.133 15.302 −7.812 1.00 19.00 A ATOM 123 CG LYS A 86 35.793 14.660 −6.481 1.00 21.55 A ATOM 124 CD LYS A 86 34.368 14.981 −6.066 1.00 26.48 A ATOM 125 CE LYS A 86 33.994 14.239 −4.793 1.00 31.92 A ATOM 126 NZ LYS A 86 32.568 14.457 −4.412 1.00 35.36 A ATOM 127 C LYS A 86 38.523 15.571 −7.202 1.00 18.57 A ATOM 128 O LYS A 86 39.045 14.807 −6.385 1.00 16.77 A ATOM 129 N ILE A 87 38.737 16.881 −7.227 1.00 17.88 A ATOM 130 CA ILE A 87 39.577 17.554 −6.256 1.00 18.26 A ATOM 131 CB ILE A 87 39.994 18.952 −6.772 1.00 19.60 A ATOM 132 CG2 ILE A 87 40.593 19.786 −5.628 1.00 18.73 A ATOM 133 CG1 ILE A 87 40.968 18.786 −7.945 1.00 21.16 A ATOM 134 CD1 ILE A 87 41.412 20.087 −8.588 1.00 25.26 A ATOM 135 C ILE A 87 38.731 17.709 −4.997 1.00 19.67 A ATOM 136 O ILE A 87 37.628 18.249 −5.052 1.00 20.41 A ATOM 137 N LEU A 88 39.240 17.229 −3.867 1.00 19.15 A ATOM 138 CA LEU A 88 38.508 17.324 −2.611 1.00 20.68 A ATOM 139 CB LEU A 88 38.870 16.151 −1.700 1.00 19.97 A ATOM 140 CG LEU A 88 38.529 14.759 −2.237 1.00 19.24 A ATOM 141 CD1 LEU A 88 39.090 13.692 −1.311 1.00 21.41 A ATOM 142 CD2 LEU A 88 37.029 14.622 −2.359 1.00 18.84 A ATOM 143 C LEU A 88 38.815 18.632 −1.901 1.00 23.11 A ATOM 144 O LEU A 88 37.999 19.146 −1.139 1.00 25.10 A ATOM 145 N GLY A 89 39.997 19.174 −2.149 1.00 24.09 A ATOM 146 CA GLY A 89 40.367 20.418 −1.507 1.00 24.27 A ATOM 147 C GLY A 89 41.658 20.954 −2.078 1.00 25.47 A ATOM 148 O GLY A 89 42.445 20.202 −2.666 1.00 22.19 A ATOM 149 N GLU A 90 41.870 22.254 −1.906 1.00 26.22 A ATOM 150 CA GLU A 90 43.064 22.924 −2.404 1.00 29.96 A ATOM 151 CB GLU A 90 42.698 23.814 −3.596 1.00 30.75 A ATOM 152 CG GLU A 90 42.267 23.038 −4.831 1.00 34.32 A ATOM 153 CD GLU A 90 41.711 23.930 −5.927 1.00 38.27 A ATOM 154 OE1 GLU A 90 40.590 24.456 −5.764 1.00 40.57 A ATOM 155 OE2 GLU A 90 42.398 24.110 −6.952 1.00 40.90 A ATOM 156 C GLU A 90 43.711 23.768 −1.313 1.00 30.68 A ATOM 157 O GLU A 90 43.049 24.574 −0.668 1.00 32.83 A ATOM 158 N GLY A 91 45.006 23.566 −1.104 1.00 29.66 A ATOM 159 CA GLY A 91 45.724 24.332 −0.104 1.00 29.40 A ATOM 160 C GLY A 91 46.795 25.151 −0.798 1.00 29.98 A ATOM 161 O GLY A 91 46.894 25.130 −2.028 1.00 28.16 A ATOM 162 N SER A 92 47.605 25.870 −0.029 1.00 28.30 A ATOM 163 CA SER A 92 48.653 26.681 −0.633 1.00 30.50 A ATOM 164 CB SER A 92 49.165 27.717 0.370 1.00 32.43 A ATOM 165 OG SER A 92 49.520 27.099 1.593 1.00 40.94 A ATOM 166 C SER A 92 49.815 25.843 −1.164 1.00 29.77 A ATOM 167 O SER A 92 50.456 26.221 −2.143 1.00 30.46 A ATOM 168 N PHE A 93 50.087 24.703 −0.536 1.00 27.65 A ATOM 169 CA PHE A 93 51.185 23.855 −0.995 1.00 26.34 A ATOM 170 CB PHE A 93 52.281 23.785 0.068 1.00 27.95 A ATOM 171 CG PHE A 93 52.861 25.117 0.406 1.00 31.06 A ATOM 172 CD1 PHE A 93 52.283 25.909 1.392 1.00 29.96 A ATOM 173 CD2 PHE A 93 53.949 25.613 −0.308 1.00 31.38 A ATOM 174 CE1 PHE A 93 52.779 27.181 1.665 1.00 32.69 A ATOM 175 CE2 PHE A 93 54.452 26.883 −0.044 1.00 32.63 A ATOM 176 CZ PHE A 93 53.864 27.670 0.945 1.00 31.81 A ATOM 177 C PHE A 93 50.759 22.445 −1.365 1.00 25.39 A ATOM 178 O PHE A 93 51.601 21.559 −1.522 1.00 24.59 A ATOM 179 N SER A 94 49.457 22.235 −1.519 1.00 23.63 A ATOM 180 CA SER A 94 48.965 20.912 −1.860 1.00 21.43 A ATOM 181 CB SER A 94 49.017 20.013 −0.628 1.00 21.42 A ATOM 182 OG SER A 94 48.091 20.475 0.340 1.00 21.19 A ATOM 183 C SER A 94 47.539 20.925 −2.378 1.00 19.82 A ATOM 184 O SER A 94 46.795 21.882 −2.173 1.00 18.76 A ATOM 185 N THR A 95 47.174 19.832 −3.038 1.00 19.38 A ATOM 186 CA THR A 95 45.840 19.637 −3.580 1.00 17.98 A ATOM 187 CB THR A 95 45.818 19.818 −5.110 1.00 19.25 A ATOM 188 OG1 THR A 95 46.196 21.162 −5.434 1.00 22.04 A ATOM 189 CG2 THR A 95 44.421 19.549 −5.661 1.00 17.61 A ATOM 190 C THR A 95 45.455 18.201 −3.243 1.00 18.61 A ATOM 191 O THR A 95 46.212 17.264 −3.524 1.00 17.10 A ATOM 192 N VAL A 96 44.295 18.024 −2.623 1.00 16.53 A ATOM 193 CA VAL A 96 43.845 16.685 −2.266 1.00 16.05 A ATOM 194 CB VAL A 96 43.170 16.672 −0.886 1.00 16.32 A ATOM 195 CG1 VAL A 96 42.741 15.249 −0.532 1.00 18.02 A ATOM 196 CG2 VAL A 96 44.145 17.206 0.168 1.00 16.69 A ATOM 197 C VAL A 96 42.875 16.207 −3.335 1.00 16.42 A ATOM 198 O VAL A 96 41.906 16.892 −3.665 1.00 16.47 A ATOM 199 N VAL A 97 43.157 15.033 −3.888 1.00 16.80 A ATOM 200 CA VAL A 97 42.338 14.471 −4.949 1.00 16.72 A ATOM 201 CB VAL A 97 43.153 14.354 −6.255 1.00 18.43 A ATOM 202 CG1 VAL A 97 42.249 13.927 −7.404 1.00 19.69 A ATOM 203 CG2 VAL A 97 43.831 15.685 −6.569 1.00 17.84 A ATOM 204 C VAL A 97 41.812 13.091 −4.583 1.00 16.77 A ATOM 205 O VAL A 97 42.532 12.270 −4.014 1.00 17.13 A ATOM 206 N LEU A 98 40.545 12.845 −4.895 1.00 16.62 A ATOM 207 CA LEU A 98 39.947 11.548 −4.624 1.00 17.04 A ATOM 208 CB LEU A 98 38.424 11.633 −4.743 1.00 16.89 A ATOM 209 CG LEU A 98 37.635 10.342 −4.508 1.00 19.46 A ATOM 210 CD1 LEU A 98 37.990 9.762 −3.146 1.00 20.07 A ATOM 211 CD2 LEU A 98 36.143 10.627 −4.588 1.00 17.93 A ATOM 212 C LEU A 98 40.512 10.597 −5.677 1.00 17.38 A ATOM 213 O LEU A 98 40.527 10.920 −6.863 1.00 18.60 A ATOM 214 N ALA A 99 40.995 9.438 −5.246 1.00 17.13 A ATOM 215 CA ALA A 99 41.570 8.466 −6.168 1.00 18.42 A ATOM 216 CB ALA A 99 43.090 8.524 −6.105 1.00 14.76 A ATOM 217 C ALA A 99 41.102 7.055 −5.848 1.00 21.40 A ATOM 218 O ALA A 99 40.941 6.691 −4.679 1.00 22.52 A ATOM 219 N ARG A 100 40.878 6.261 −6.888 1.00 19.77 A ATOM 220 CA ARG A 100 40.459 4.884 −6.693 1.00 20.85 A ATOM 221 CB ARG A 100 39.202 4.585 −7.518 1.00 24.22 A ATOM 222 CG ARG A 100 38.608 3.205 −7.256 1.00 31.78 A ATOM 223 CD ARG A 100 37.326 2.979 −8.048 1.00 36.24 A ATOM 224 NE ARG A 100 36.213 3.818 −7.594 1.00 41.40 A ATOM 225 CZ ARG A 100 35.566 3.662 −6.439 1.00 42.05 A ATOM 226 NH1 ARG A 100 35.912 2.696 −5.598 1.00 40.67 A ATOM 227 NH2 ARG A 100 34.559 4.468 −6.128 1.00 43.65 A ATOM 228 C ARG A 100 41.613 3.985 −7.129 1.00 18.63 A ATOM 229 O ARG A 100 42.078 4.065 −8.271 1.00 19.49 A ATOM 230 N GLU A 101 42.102 3.157 −6.212 1.00 16.43 A ATOM 231 CA GLU A 101 43.196 2.246 −6.533 1.00 16.11 A ATOM 232 CB GLU A 101 43.774 1.637 −5.248 1.00 16.79 A ATOM 233 CG GLU A 101 44.917 0.657 −5.488 1.00 16.51 A ATOM 234 CD GLU A 101 45.501 0.115 −4.200 1.00 18.20 A ATOM 235 OE1 GLU A 101 44.733 −0.081 −3.239 1.00 18.32 A ATOM 236 OE2 GLU A 101 46.725 −0.132 −4.150 1.00 17.14 A ATOM 237 C GLU A 101 42.625 1.152 −7.442 1.00 17.92 A ATOM 238 O GLU A 101 41.681 0.462 −7.069 1.00 18.02 A ATOM 239 N LEU A 102 43.198 1.002 −8.632 1.00 19.06 A ATOM 240 CA LEU A 102 42.718 0.025 −9.607 1.00 20.71 A ATOM 241 CB LEU A 102 43.569 0.097 −10.878 1.00 23.42 A ATOM 242 CG LEU A 102 43.531 1.426 −11.642 1.00 25.30 A ATOM 243 CD1 LEU A 102 44.577 1.414 −12.748 1.00 27.88 A ATOM 244 CD2 LEU A 102 42.140 1.647 −12.214 1.00 26.79 A ATOM 245 C LEU A 102 42.671 −1.418 −9.125 1.00 21.62 A ATOM 246 O LEU A 102 41.668 −2.103 −9.305 1.00 21.09 A ATOM 247 N ALA A 103 43.753 −1.874 −8.507 1.00 19.38 A ATOM 248 CA ALA A 103 43.836 −3.249 −8.035 1.00 20.87 A ATOM 249 CB ALA A 103 45.284 −3.571 −7.671 1.00 19.23 A ATOM 250 C ALA A 103 42.919 −3.629 −6.872 1.00 19.92 A ATOM 251 O ALA A 103 42.703 −4.815 −6.628 1.00 20.38 A ATOM 252 N THR A 104 42.361 −2.643 −6.175 1.00 18.12 A ATOM 253 CA THR A 104 41.517 −2.927 −5.018 1.00 17.15 A ATOM 254 CB THR A 104 42.212 −2.484 −3.717 1.00 19.54 A ATOM 255 OG1 THR A 104 42.456 −1.070 −3.773 1.00 19.26 A ATOM 256 CG2 THR A 104 43.536 −3.219 −3.529 1.00 17.02 A ATOM 257 C THR A 104 40.159 −2.247 −5.026 1.00 19.44 A ATOM 258 O THR A 104 39.259 −2.648 −4.285 1.00 18.70 A ATOM 259 N SER A 105 40.034 −1.207 −5.847 1.00 19.65 A ATOM 260 CA SER A 105 38.819 −0.400 −5.967 1.00 19.37 A ATOM 261 CB SER A 105 37.598 −1.304 −6.173 1.00 21.81 A ATOM 262 OG SER A 105 36.431 −0.539 −6.412 1.00 23.01 A ATOM 263 C SER A 105 38.644 0.447 −4.701 1.00 18.99 A ATOM 264 O SER A 105 37.602 1.070 −4.488 1.00 18.66 A ATOM 265 N ARG A 106 39.674 0.468 −3.861 1.00 16.84 A ATOM 266 CA ARG A 106 39.655 1.267 −2.634 1.00 16.21 A ATOM 267 CB ARG A 106 40.827 0.886 −1.723 1.00 16.41 A ATOM 268 CG ARG A 106 40.619 −0.367 −0.906 1.00 15.49 A ATOM 269 CD ARG A 106 41.887 −0.755 −0.170 1.00 17.43 A ATOM 270 NE ARG A 106 41.620 −1.792 0.824 1.00 20.47 A ATOM 271 CZ ARG A 106 42.548 −2.568 1.371 1.00 20.24 A ATOM 272 NH1 ARG A 106 43.821 −2.433 1.017 1.00 17.80 A ATOM 273 NH2 ARG A 106 42.198 −3.468 2.285 1.00 20.14 A ATOM 274 C ARG A 106 39.785 2.746 −2.981 1.00 17.37 A ATOM 275 O ARG A 106 40.514 3.103 −3.902 1.00 17.75 A ATOM 276 N GLU A 107 39.085 3.599 −2.240 1.00 16.06 A ATOM 277 CA GLU A 107 39.156 5.039 −2.461 1.00 20.80 A ATOM 278 CB GLU A 107 37.779 5.694 −2.337 1.00 22.93 A ATOM 279 CG GLU A 107 36.711 5.171 −3.269 1.00 30.87 A ATOM 280 CD GLU A 107 35.431 5.975 −3.148 1.00 32.40 A ATOM 281 OE1 GLU A 107 35.262 6.939 −3.923 1.00 33.74 A ATOM 282 OE2 GLU A 107 34.608 5.654 −2.263 1.00 36.00 A ATOM 283 C GLU A 107 40.053 5.678 −1.410 1.00 18.93 A ATOM 284 O GLU A 107 39.891 5.427 −0.220 1.00 19.21 A ATOM 285 N TYR A 108 40.988 6.507 −1.852 1.00 16.70 A ATOM 286 CA TYR A 108 41.883 7.209 −0.942 1.00 15.86 A ATOM 287 CB TYR A 108 43.325 6.728 −1.104 1.00 15.30 A ATOM 288 CG TYR A 108 43.593 5.328 −0.612 1.00 16.33 A ATOM 289 CD1 TYR A 108 43.765 5.066 0.746 1.00 16.36 A ATOM 290 CE1 TYR A 108 44.046 3.769 1.201 1.00 18.48 A ATOM 291 CD2 TYR A 108 43.701 4.268 −1.511 1.00 13.25 A ATOM 292 CE2 TYR A 108 43.980 2.981 −1.075 1.00 17.28 A ATOM 293 CZ TYR A 108 44.152 2.736 0.276 1.00 19.17 A ATOM 294 OH TYR A 108 44.440 1.461 0.688 1.00 19.38 A ATOM 295 C TYR A 108 41.850 8.687 −1.292 1.00 16.80 A ATOM 296 O TYR A 108 41.560 9.058 −2.431 1.00 15.22 A ATOM 297 N ALA A 109 42.132 9.528 −0.306 1.00 14.61 A ATOM 298 CA ALA A 109 42.207 10.957 −0.539 1.00 14.30 A ATOM 299 CB ALA A 109 41.671 11.726 0.661 1.00 14.78 A ATOM 300 C ALA A 109 43.713 11.136 −0.667 1.00 16.79 A ATOM 301 O ALA A 109 44.450 10.983 0.317 1.00 16.52 A ATOM 302 N ILE A 110 44.182 11.410 −1.881 1.00 14.80 A ATOM 303 CA ILE A 110 45.609 11.574 −2.093 1.00 15.80 A ATOM 304 CB ILE A 110 46.065 10.863 −3.396 1.00 16.85 A ATOM 305 CG2 ILE A 110 47.550 11.098 −3.632 1.00 16.80 A ATOM 306 CG1 ILE A 110 45.774 9.358 −3.284 1.00 17.76 A ATOM 307 CD1 ILE A 110 46.308 8.513 −4.437 1.00 16.07 A ATOM 308 C ILE A 110 46.004 13.045 −2.129 1.00 17.78 A ATOM 309 O ILE A 110 45.534 13.813 −2.976 1.00 16.24 A ATOM 310 N LYS A 111 46.846 13.435 −1.177 1.00 16.15 A ATOM 311 CA LYS A 111 47.326 14.808 −1.100 1.00 17.20 A ATOM 312 CB LYS A 111 47.700 15.176 0.344 1.00 17.41 A ATOM 313 CG LYS A 111 48.350 16.547 0.464 1.00 20.71 A ATOM 314 CD LYS A 111 48.585 16.971 1.910 1.00 24.25 A ATOM 315 CE LYS A 111 47.288 17.381 2.598 1.00 29.46 A ATOM 316 NZ LYS A 111 47.516 17.866 4.000 1.00 30.50 A ATOM 317 C LYS A 111 48.551 14.890 −1.994 1.00 16.41 A ATOM 318 O LYS A 111 49.509 14.137 −1.813 1.00 18.20 A ATOM 319 N ILE A 112 48.509 15.798 −2.963 1.00 15.87 A ATOM 320 CA ILE A 112 49.606 15.967 −3.907 1.00 17.28 A ATOM 321 CB ILE A 112 49.079 15.911 −5.358 1.00 16.43 A ATOM 322 CG2 ILE A 112 50.235 15.998 −6.341 1.00 15.12 A ATOM 323 CG1 ILE A 112 48.293 14.609 −5.565 1.00 16.82 A ATOM 324 CD1 ILE A 112 47.580 14.511 −6.904 1.00 18.47 A ATOM 325 C ILE A 112 50.307 17.301 −3.663 1.00 19.03 A ATOM 326 O ILE A 112 49.669 18.350 −3.635 1.00 19.15 A ATOM 327 N LEU A 113 51.622 17.245 −3.472 1.00 20.22 A ATOM 328 CA LEU A 113 52.416 18.442 −3.214 1.00 22.36 A ATOM 329 CB LEU A 113 52.995 18.397 −1.794 1.00 22.13 A ATOM 330 CG LEU A 113 52.042 18.063 −0.646 1.00 22.46 A ATOM 331 CD1 LEU A 113 51.866 16.557 −0.553 1.00 23.81 A ATOM 332 CD2 LEU A 113 52.603 18.595 0.660 1.00 23.68 A ATOM 333 C LEU A 113 53.560 18.547 −4.215 1.00 23.37 A ATOM 334 O LEU A 113 54.300 17.586 −4.424 1.00 23.11 A ATOM 335 N GLU A 114 53.706 19.714 −4.834 1.00 23.88 A ATOM 336 CA GLU A 114 54.771 19.920 −5.806 1.00 26.00 A ATOM 337 CB GLU A 114 54.435 21.111 −6.706 1.00 27.74 A ATOM 338 CG GLU A 114 55.533 21.452 −7.696 1.00 35.07 A ATOM 339 CD GLU A 114 55.220 22.696 −8.497 1.00 39.24 A ATOM 340 OE1 GLU A 114 54.808 23.703 −7.885 1.00 41.45 A ATOM 341 OE2 GLU A 114 55.395 22.670 −9.736 1.00 44.05 A ATOM 342 C GLU A 114 56.087 20.163 −5.067 1.00 24.37 A ATOM 343 O GLU A 114 56.186 21.071 −4.238 1.00 24.43 A ATOM 344 N LYS A 115 57.096 19.350 −5.360 1.00 24.10 A ATOM 345 CA LYS A 115 58.376 19.493 −4.678 1.00 24.93 A ATOM 346 CB LYS A 115 59.339 18.373 −5.103 1.00 23.72 A ATOM 347 CG LYS A 115 59.139 17.080 −4.308 1.00 23.09 A ATOM 348 CD LYS A 115 60.064 15.944 −4.743 1.00 21.92 A ATOM 349 CE LYS A 115 59.691 15.400 −6.117 1.00 22.42 A ATOM 350 NZ LYS A 115 60.447 14.150 −6.448 1.00 19.71 A ATOM 351 C LYS A 115 59.031 20.858 −4.868 1.00 26.87 A ATOM 352 O LYS A 115 59.492 21.469 −3.903 1.00 26.17 A ATOM 353 N ARG A 116 59.058 21.348 −6.102 1.00 28.73 A ATOM 354 CA ARG A 116 59.678 22.638 −6.380 1.00 29.66 A ATOM 355 CB ARG A 116 59.533 22.980 −7.868 1.00 31.29 A ATOM 356 CG ARG A 116 60.047 24.361 −8.267 1.00 33.19 A ATOM 357 CD ARG A 116 61.368 24.710 −7.590 1.00 35.13 A ATOM 358 NE ARG A 116 62.329 23.612 −7.618 1.00 36.42 A ATOM 359 CZ ARG A 116 63.510 23.648 −7.009 1.00 36.18 A ATOM 360 NH1 ARG A 116 63.871 24.729 −6.332 1.00 36.12 A ATOM 361 NH2 ARG A 116 64.324 22.602 −7.067 1.00 35.77 A ATOM 362 C ARG A 116 59.097 23.761 −5.519 1.00 29.70 A ATOM 363 O ARG A 116 59.843 24.515 −4.889 1.00 29.16 A ATOM 364 N HIS A 117 57.773 23.862 −5.472 1.00 27.22 A ATOM 365 CA HIS A 117 57.126 24.903 −4.681 1.00 26.33 A ATOM 366 CB HIS A 117 55.606 24.835 −4.848 1.00 28.41 A ATOM 367 CG HIS A 117 54.881 26.005 −4.258 1.00 31.82 A ATOM 368 CD2 HIS A 117 55.309 27.249 −3.935 1.00 33.19 A ATOM 369 ND1 HIS A 117 53.536 25.974 −3.961 1.00 34.30 A ATOM 370 CE1 HIS A 117 53.165 27.148 −3.480 1.00 34.58 A ATOM 371 NE2 HIS A 117 54.222 27.940 −3.455 1.00 35.18 A ATOM 372 C HIS A 117 57.477 24.780 −3.202 1.00 26.22 A ATOM 373 O HIS A 117 57.737 25.776 −2.534 1.00 25.67 A ATOM 374 N ILE A 118 57.469 23.554 −2.689 1.00 24.94 A ATOM 375 CA ILE A 118 57.792 23.315 −1.285 1.00 23.94 A ATOM 376 CB ILE A 118 57.711 21.812 −0.952 1.00 23.50 A ATOM 377 CG2 ILE A 118 58.374 21.533 0.389 1.00 23.76 A ATOM 378 CG1 ILE A 118 56.246 21.362 −0.959 1.00 24.42 A ATOM 379 CD1 ILE A 118 56.066 19.858 −0.834 1.00 28.06 A ATOM 380 C ILE A 118 59.195 23.821 −0.958 1.00 23.78 A ATOM 381 O ILE A 118 59.402 24.495 0.048 1.00 23.49 A ATOM 382 N ILE A 119 60.153 23.489 −1.815 1.00 23.46 A ATOM 383 CA ILE A 119 61.534 23.913 −1.619 1.00 25.13 A ATOM 384 CB ILE A 119 62.467 23.250 −2.664 1.00 24.25 A ATOM 385 CG2 ILE A 119 63.858 23.890 −2.617 1.00 22.47 A ATOM 386 CG1 ILE A 119 62.540 21.738 −2.395 1.00 25.05 A ATOM 387 CD1 ILE A 119 63.327 20.945 −3.439 1.00 24.62 A ATOM 388 C ILE A 119 61.667 25.435 −1.705 1.00 25.96 A ATOM 389 O ILE A 119 62.330 26.051 −0.872 1.00 24.78 A ATOM 390 N LYS A 120 61.028 26.039 −2.704 1.00 27.67 A ATOM 391 CA LYS A 120 61.100 27.489 −2.879 1.00 30.29 A ATOM 392 CB LYS A 120 60.242 27.940 −4.060 1.00 32.34 A ATOM 393 CG LYS A 120 60.674 27.407 −5.409 1.00 39.30 A ATOM 394 CD LYS A 120 59.765 27.950 −6.512 1.00 45.19 A ATOM 395 CE LYS A 120 58.294 27.636 −6.218 1.00 46.48 A ATOM 396 NZ LYS A 120 57.363 28.155 −7.252 1.00 46.49 A ATOM 397 C LYS A 120 60.647 28.247 −1.638 1.00 30.89 A ATOM 398 O LYS A 120 61.303 29.198 −1.217 1.00 32.48 A ATOM 399 N GLU A 121 59.527 27.825 −1.055 1.00 29.82 A ATOM 400 CA GLU A 121 58.986 28.488 0.128 1.00 30.33 A ATOM 401 CB GLU A 121 57.455 28.416 0.117 1.00 33.04 A ATOM 402 CG GLU A 121 56.794 29.021 −1.120 1.00 36.45 A ATOM 403 CD GLU A 121 57.221 30.456 −1.373 1.00 39.88 A ATOM 404 OE1 GLU A 121 57.200 31.264 −0.420 1.00 40.53 A ATOM 405 OE2 GLU A 121 57.573 30.778 −2.529 1.00 43.24 A ATOM 406 C GLU A 121 59.511 27.930 1.451 1.00 30.37 A ATOM 407 O GLU A 121 58.946 28.204 2.513 1.00 31.24 A ATOM 408 N ASN A 122 60.588 27.151 1.390 1.00 29.03 A ATOM 409 CA ASN A 122 61.183 26.573 2.594 1.00 28.46 A ATOM 410 CB ASN A 122 61.836 27.673 3.436 1.00 31.28 A ATOM 411 CG ASN A 122 62.945 28.395 2.698 1.00 34.12 A ATOM 412 OD1 ASN A 122 62.697 29.143 1.754 1.00 35.57 A ATOM 413 ND2 ASN A 122 64.181 28.169 3.127 1.00 35.73 A ATOM 414 C ASN A 122 60.157 25.835 3.456 1.00 26.89 A ATOM 415 O ASN A 122 60.085 26.055 4.663 1.00 27.23 A ATOM 416 N LYS A 123 59.375 24.955 2.842 1.00 23.99 A ATOM 417 CA LYS A 123 58.358 24.210 3.574 1.00 22.43 A ATOM 418 CB LYS A 123 57.031 24.248 2.810 1.00 21.97 A ATOM 419 CG LYS A 123 56.475 25.645 2.599 1.00 25.68 A ATOM 420 CD LYS A 123 56.253 26.354 3.927 1.00 27.54 A ATOM 421 CE LYS A 123 55.822 27.796 3.716 1.00 31.30 A ATOM 422 NZ LYS A 123 55.756 28.540 5.004 1.00 33.21 A ATOM 423 C LYS A 123 58.748 22.759 3.821 1.00 22.20 A ATOM 424 O LYS A 123 57.924 21.960 4.264 1.00 22.50 A ATOM 425 N VAL A 124 59.997 22.412 3.535 1.00 20.59 A ATOM 426 CA VAL A 124 60.439 21.039 3.730 1.00 20.25 A ATOM 427 CB VAL A 124 61.922 20.850 3.328 1.00 19.43 A ATOM 428 CG1 VAL A 124 62.346 19.407 3.573 1.00 18.69 A ATOM 429 CG2 VAL A 124 62.104 21.195 1.853 1.00 18.21 A ATOM 430 C VAL A 124 60.236 20.561 5.163 1.00 19.53 A ATOM 431 O VAL A 124 59.841 19.418 5.385 1.00 20.02 A ATOM 432 N PRO A 125 60.513 21.422 6.159 1.00 20.01 A ATOM 433 CD PRO A 125 61.178 22.738 6.118 1.00 18.69 A ATOM 434 CA PRO A 125 60.318 20.979 7.544 1.00 19.88 A ATOM 435 CB PRO A 125 60.793 22.180 8.363 1.00 19.95 A ATOM 436 CG PRO A 125 61.839 22.805 7.479 1.00 18.85 A ATOM 437 C PRO A 125 58.848 20.642 7.824 1.00 19.76 A ATOM 438 O PRO A 125 58.544 19.700 8.550 1.00 16.99 A ATOM 439 N TYR A 126 57.947 21.418 7.235 1.00 18.98 A ATOM 440 CA TYR A 126 56.516 21.220 7.435 1.00 21.97 A ATOM 441 CB TYR A 126 55.752 22.448 6.933 1.00 25.17 A ATOM 442 CG TYR A 126 56.040 23.690 7.748 1.00 30.98 A ATOM 443 CD1 TYR A 126 55.438 23.886 8.991 1.00 33.95 A ATOM 444 CE1 TYR A 126 55.721 25.015 9.763 1.00 36.60 A ATOM 445 CD2 TYR A 126 56.938 24.657 7.292 1.00 35.43 A ATOM 446 CE2 TYR A 126 57.231 25.792 8.058 1.00 37.20 A ATOM 447 CZ TYR A 126 56.618 25.962 9.291 1.00 37.40 A ATOM 448 OH TYR A 126 56.903 27.073 10.052 1.00 40.85 A ATOM 449 C TYR A 126 55.990 19.956 6.762 1.00 21.35 A ATOM 450 O TYR A 126 55.265 19.175 7.383 1.00 20.49 A ATOM 451 N VAL A 127 56.354 19.746 5.501 1.00 18.16 A ATOM 452 CA VAL A 127 55.892 18.562 4.790 1.00 17.58 A ATOM 453 CB VAL A 127 56.308 18.596 3.308 1.00 17.45 A ATOM 454 CG1 VAL A 127 55.786 17.350 2.600 1.00 17.97 A ATOM 455 CG2 VAL A 127 55.751 19.850 2.641 1.00 14.90 A ATOM 456 C VAL A 127 56.459 17.306 5.448 1.00 18.39 A ATOM 457 O VAL A 127 55.769 16.298 5.583 1.00 18.14 A ATOM 458 N THR A 128 57.716 17.381 5.869 1.00 17.50 A ATOM 459 CA THR A 128 58.375 16.260 6.530 1.00 18.54 A ATOM 460 CB THR A 128 59.861 16.586 6.805 1.00 18.01 A ATOM 461 OG1 THR A 128 60.537 16.804 5.559 1.00 21.14 A ATOM 462 CG2 THR A 128 60.536 15.446 7.545 1.00 17.95 A ATOM 463 C THR A 128 57.676 15.941 7.856 1.00 19.49 A ATOM 464 O THR A 128 57.438 14.776 8.179 1.00 18.76 A ATOM 465 N ARG A 129 57.345 16.981 8.619 1.00 19.60 A ATOM 466 CA ARG A 129 56.673 16.804 9.904 1.00 20.12 A ATOM 467 CB ARG A 129 56.534 18.144 10.621 1.00 21.33 A ATOM 468 CG ARG A 129 55.948 18.029 12.023 1.00 28.02 A ATOM 469 CD ARG A 129 55.721 19.404 12.597 1.00 31.25 A ATOM 470 NE ARG A 129 56.940 20.205 12.560 1.00 37.78 A ATOM 471 CZ ARG A 129 56.962 21.524 12.391 1.00 40.10 A ATOM 472 NH1 ARG A 129 55.828 22.197 12.239 1.00 40.03 A ATOM 473 NH2 ARG A 129 58.119 22.170 12.374 1.00 44.58 A ATOM 474 C ARG A 129 55.288 16.186 9.729 1.00 20.08 A ATOM 475 O ARG A 129 54.891 15.305 10.496 1.00 20.40 A ATOM 476 N GLU A 130 54.553 16.654 8.724 1.00 18.79 A ATOM 477 CA GLU A 130 53.222 16.125 8.454 1.00 20.10 A ATOM 478 CB GLU A 130 52.638 16.749 7.183 1.00 19.92 A ATOM 479 CG GLU A 130 51.350 16.087 6.708 1.00 27.85 A ATOM 480 CD GLU A 130 50.581 16.933 5.707 1.00 29.72 A ATOM 481 OE1 GLU A 130 51.216 17.528 4.814 1.00 33.46 A ATOM 482 OE2 GLU A 130 49.339 16.996 5.807 1.00 30.74 A ATOM 483 C GLU A 130 53.301 14.615 8.295 1.00 19.81 A ATOM 484 O GLU A 130 52.553 13.875 8.935 1.00 18.37 A ATOM 485 N ARG A 131 54.219 14.162 7.447 1.00 20.41 A ATOM 486 CA ARG A 131 54.397 12.735 7.202 1.00 22.45 A ATOM 487 CB ARG A 131 55.442 12.511 6.098 1.00 25.16 A ATOM 488 CG ARG A 131 55.742 11.043 5.840 1.00 28.75 A ATOM 489 CD ARG A 131 56.736 10.837 4.708 1.00 33.75 A ATOM 490 NE ARG A 131 57.020 9.415 4.520 1.00 40.07 A ATOM 491 CZ ARG A 131 57.756 8.915 3.532 1.00 43.07 A ATOM 492 NH1 ARG A 131 58.293 9.721 2.625 1.00 44.91 A ATOM 493 NH2 ARG A 131 57.955 7.606 3.449 1.00 44.45 A ATOM 494 C ARG A 131 54.820 11.982 8.466 1.00 23.24 A ATOM 495 O ARG A 131 54.241 10.948 8.804 1.00 23.86 A ATOM 496 N ASP A 132 55.831 12.497 9.160 1.00 21.99 A ATOM 497 CA ASP A 132 56.318 11.850 10.370 1.00 22.04 A ATOM 498 CB ASP A 132 57.570 12.564 10.888 1.00 23.72 A ATOM 499 CG ASP A 132 58.750 12.442 9.932 1.00 27.77 A ATOM 500 OD1 ASP A 132 58.681 11.620 8.989 1.00 27.34 A ATOM 501 OD2 ASP A 132 59.753 13.163 10.128 1.00 28.70 A ATOM 502 C ASP A 132 55.258 11.772 11.474 1.00 21.69 A ATOM 503 O ASP A 132 55.077 10.723 12.092 1.00 22.75 A ATOM 504 N VAL A 133 54.551 12.868 11.725 1.00 19.54 A ATOM 505 CA VAL A 133 53.525 12.843 12.759 1.00 18.52 A ATOM 506 CB VAL A 133 52.908 14.244 12.990 1.00 19.26 A ATOM 507 CG1 VAL A 133 51.708 14.135 13.918 1.00 18.79 A ATOM 508 CG2 VAL A 133 53.953 15.180 13.604 1.00 18.80 A ATOM 509 C VAL A 133 52.419 11.854 12.398 1.00 19.46 A ATOM 510 O VAL A 133 52.073 10.991 13.200 1.00 19.94 A ATOM 511 N MET A 134 51.878 11.957 11.187 1.00 19.15 A ATOM 512 CA MET A 134 50.807 11.052 10.792 1.00 21.25 A ATOM 513 CB MET A 134 50.309 11.381 9.383 1.00 17.34 A ATOM 514 CG MET A 134 49.615 12.730 9.302 1.00 20.00 A ATOM 515 SD MET A 134 48.643 12.952 7.798 1.00 24.21 A ATOM 516 CE MET A 134 47.033 12.434 8.400 1.00 23.20 A ATOM 517 C MET A 134 51.203 9.582 10.881 1.00 22.43 A ATOM 518 O MET A 134 50.384 8.741 11.249 1.00 23.82 A ATOM 519 N SER A 135 52.454 9.273 10.556 1.00 23.09 A ATOM 520 CA SER A 135 52.939 7.895 10.615 1.00 26.13 A ATOM 521 CB SER A 135 54.356 7.798 10.039 1.00 26.17 A ATOM 522 OG SER A 135 54.383 8.177 8.673 1.00 31.91 A ATOM 523 C SER A 135 52.957 7.358 12.045 1.00 26.58 A ATOM 524 O SER A 135 52.926 6.148 12.261 1.00 26.42 A ATOM 525 N ARG A 136 53.014 8.261 13.018 1.00 25.65 A ATOM 526 CA ARG A 136 53.056 7.870 14.425 1.00 27.47 A ATOM 527 CB ARG A 136 53.823 8.914 15.238 1.00 27.97 A ATOM 528 CG ARG A 136 55.283 9.082 14.857 1.00 32.00 A ATOM 529 CD ARG A 136 55.904 10.218 15.664 1.00 33.03 A ATOM 530 NE ARG A 136 55.602 10.073 17.084 1.00 36.11 A ATOM 531 CZ ARG A 136 55.867 10.990 18.007 1.00 39.74 A ATOM 532 NH1 ARG A 136 56.449 12.132 17.661 1.00 40.55 A ATOM 533 NH2 ARG A 136 55.540 10.769 19.276 1.00 36.72 A ATOM 534 C ARG A 136 51.667 7.709 15.036 1.00 26.38 A ATOM 535 O ARG A 136 51.516 7.121 16.106 1.00 27.06 A ATOM 536 N LEU A 137 50.655 8.235 14.360 1.00 24.77 A ATOM 537 CA LEU A 137 49.294 8.162 14.870 1.00 24.70 A ATOM 538 CB LEU A 137 48.483 9.363 14.371 1.00 24.52 A ATOM 539 CG LEU A 137 49.050 10.760 14.662 1.00 26.67 A ATOM 540 CD1 LEU A 137 48.075 11.813 14.141 1.00 27.25 A ATOM 541 CD2 LEU A 137 49.279 10.945 16.155 1.00 27.09 A ATOM 542 C LEU A 137 48.592 6.868 14.473 1.00 25.20 A ATOM 543 O LEU A 137 48.619 6.469 13.309 1.00 25.99 A ATOM 544 N ASP A 138 47.971 6.218 15.451 1.00 21.89 A ATOM 545 CA ASP A 138 47.239 4.977 15.219 1.00 21.35 A ATOM 546 CB ASP A 138 48.124 3.761 15.523 1.00 22.14 A ATOM 547 CG ASP A 138 47.432 2.448 15.201 1.00 24.90 A ATOM 548 OD1 ASP A 138 46.631 2.423 14.241 1.00 24.78 A ATOM 549 OD2 ASP A 138 47.691 1.443 15.897 1.00 25.39 A ATOM 550 C ASP A 138 46.031 4.991 16.138 1.00 20.47 A ATOM 551 O ASP A 138 45.967 4.248 17.118 1.00 19.06 A ATOM 552 N HIS A 139 45.075 5.852 15.810 1.00 18.27 A ATOM 553 CA HIS A 139 43.869 6.016 16.606 1.00 18.21 A ATOM 554 CB HIS A 139 44.096 7.157 17.612 1.00 15.84 A ATOM 555 CG HIS A 139 42.985 7.332 18.600 1.00 15.24 A ATOM 556 CD2 HIS A 139 42.884 6.964 19.900 1.00 13.97 A ATOM 557 ND1 HIS A 139 41.791 7.943 18.280 1.00 14.74 A ATOM 558 CE1 HIS A 139 41.002 7.944 19.341 1.00 14.19 A ATOM 559 NE2 HIS A 139 41.641 7.356 20.336 1.00 14.15 A ATOM 560 C HIS A 139 42.715 6.330 15.654 1.00 18.50 A ATOM 561 O HIS A 139 42.879 7.080 14.693 1.00 20.80 A ATOM 562 N PRO A 140 41.527 5.767 15.913 1.00 18.32 A ATOM 563 CD PRO A 140 41.143 4.984 17.100 1.00 16.71 A ATOM 564 CA PRO A 140 40.367 6.001 15.048 1.00 17.43 A ATOM 565 CB PRO A 140 39.273 5.157 15.704 1.00 16.64 A ATOM 566 CG PRO A 140 39.643 5.204 17.152 1.00 18.43 A ATOM 567 C PRO A 140 39.914 7.441 14.803 1.00 18.77 A ATOM 568 O PRO A 140 39.207 7.695 13.831 1.00 19.88 A ATOM 569 N PHE A 141 40.301 8.381 15.664 1.00 17.14 A ATOM 570 CA PHE A 141 39.874 9.767 15.477 1.00 16.42 A ATOM 571 CB PHE A 141 39.568 10.422 16.836 1.00 14.60 A ATOM 572 CG PHE A 141 38.386 9.817 17.556 1.00 15.26 A ATOM 573 CD1 PHE A 141 37.335 9.234 16.842 1.00 14.78 A ATOM 574 CD2 PHE A 141 38.297 9.880 18.942 1.00 13.70 A ATOM 575 CE1 PHE A 141 36.215 8.727 17.502 1.00 16.94 A ATOM 576 CE2 PHE A 141 37.178 9.375 19.615 1.00 15.75 A ATOM 577 CZ PHE A 141 36.135 8.799 18.893 1.00 16.89 A ATOM 578 C PHE A 141 40.857 10.641 14.694 1.00 16.15 A ATOM 579 O PHE A 141 40.799 11.871 14.761 1.00 17.35 A ATOM 580 N PHE A 142 41.748 10.011 13.941 1.00 15.88 A ATOM 581 CA PHE A 142 42.727 10.756 13.154 1.00 17.89 A ATOM 582 CB PHE A 142 44.115 10.645 13.793 1.00 17.57 A ATOM 583 CG PHE A 142 44.240 11.371 15.103 1.00 18.74 A ATOM 584 CD1 PHE A 142 44.559 12.726 15.135 1.00 17.77 A ATOM 585 CD2 PHE A 142 43.997 10.711 16.304 1.00 18.74 A ATOM 586 CE1 PHE A 142 44.632 13.417 16.347 1.00 15.77 A ATOM 587 CE2 PHE A 142 44.065 11.393 17.522 1.00 17.56 A ATOM 588 CZ PHE A 142 44.383 12.747 17.542 1.00 17.14 A ATOM 589 C PHE A 142 42.793 10.231 11.729 1.00 19.12 A ATOM 590 O PHE A 142 42.659 9.030 11.504 1.00 20.01 A ATOM 591 N VAL A 143 42.978 11.135 10.769 1.00 18.72 A ATOM 592 CA VAL A 143 43.102 10.735 9.371 1.00 18.52 A ATOM 593 CB VAL A 143 43.294 11.961 8.440 1.00 20.66 A ATOM 594 CG1 VAL A 143 43.843 11.521 7.080 1.00 21.29 A ATOM 595 CG2 VAL A 143 41.958 12.673 8.252 1.00 22.97 A ATOM 596 C VAL A 143 44.342 9.865 9.330 1.00 18.68 A ATOM 597 O VAL A 143 45.355 10.199 9.943 1.00 18.42 A ATOM 598 N LYS A 144 44.259 8.745 8.623 1.00 18.30 A ATOM 599 CA LYS A 144 45.384 7.824 8.535 1.00 18.78 A ATOM 600 CB LYS A 144 44.889 6.373 8.608 1.00 22.27 A ATOM 601 CG LYS A 144 46.017 5.340 8.557 1.00 29.72 A ATOM 602 CD LYS A 144 45.491 3.912 8.674 1.00 34.16 A ATOM 603 CE LYS A 144 46.631 2.896 8.577 1.00 37.67 A ATOM 604 NZ LYS A 144 46.138 1.484 8.629 1.00 39.02 A ATOM 605 C LYS A 144 46.192 8.002 7.261 1.00 18.53 A ATOM 606 O LYS A 144 45.643 8.314 6.200 1.00 18.18 A ATOM 607 N LEU A 145 47.502 7.816 7.385 1.00 16.79 A ATOM 608 CA LEU A 145 48.411 7.900 6.251 1.00 17.45 A ATOM 609 CB LEU A 145 49.686 8.653 6.641 1.00 18.82 A ATOM 610 CG LEU A 145 50.734 8.902 5.549 1.00 20.23 A ATOM 611 CD1 LEU A 145 51.836 9.799 6.093 1.00 18.83 A ATOM 612 CD2 LEU A 145 51.317 7.581 5.069 1.00 19.79 A ATOM 613 C LEU A 145 48.739 6.450 5.907 1.00 19.19 A ATOM 614 O LEU A 145 49.451 5.772 6.659 1.00 17.36 A ATOM 615 N TYR A 146 48.215 5.972 4.782 1.00 17.28 A ATOM 616 CA TYR A 146 48.444 4.593 4.358 1.00 17.57 A ATOM 617 CB TYR A 146 47.288 4.098 3.486 1.00 17.74 A ATOM 618 CG TYR A 146 45.981 3.926 4.214 1.00 17.50 A ATOM 619 CD1 TYR A 146 45.099 4.995 4.377 1.00 16.50 A ATOM 620 CE1 TYR A 146 43.881 4.827 5.039 1.00 17.10 A ATOM 621 CD2 TYR A 146 45.620 2.686 4.735 1.00 18.28 A ATOM 622 CE2 TYR A 146 44.411 2.506 5.399 1.00 19.84 A ATOM 623 CZ TYR A 146 43.547 3.576 5.544 1.00 17.53 A ATOM 624 OH TYR A 146 42.342 3.376 6.169 1.00 20.67 A ATOM 625 C TYR A 146 49.735 4.376 3.582 1.00 18.72 A ATOM 626 O TYR A 146 50.382 3.338 3.715 1.00 19.51 A ATOM 627 N PHE A 147 50.110 5.350 2.765 1.00 18.09 A ATOM 628 CA PHE A 147 51.307 5.203 1.952 1.00 17.20 A ATOM 629 CB PHE A 147 51.007 4.258 0.783 1.00 16.77 A ATOM 630 CG PHE A 147 49.835 4.699 −0.070 1.00 17.75 A ATOM 631 CD1 PHE A 147 49.967 5.752 −0.975 1.00 16.58 A ATOM 632 CD2 PHE A 147 48.595 4.075 0.053 1.00 18.07 A ATOM 633 CE1 PHE A 147 48.886 6.178 −1.742 1.00 19.62 A ATOM 634 CE2 PHE A 147 47.503 4.492 −0.710 1.00 18.56 A ATOM 635 CZ PHE A 147 47.647 5.546 −1.610 1.00 19.27 A ATOM 636 C PHE A 147 51.768 6.533 1.395 1.00 17.13 A ATOM 637 O PHE A 147 51.045 7.528 1.452 1.00 14.43 A ATOM 638 N THR A 148 52.981 6.534 0.854 1.00 17.12 A ATOM 639 CA THR A 148 53.541 7.718 0.232 1.00 17.96 A ATOM 640 CB THR A 148 54.449 8.531 1.197 1.00 21.51 A ATOM 641 OG1 THR A 148 55.605 7.760 1.537 1.00 18.83 A ATOM 642 CG2 THR A 148 53.700 8.897 2.472 1.00 19.60 A ATOM 643 C THR A 148 54.386 7.262 −0.946 1.00 20.31 A ATOM 644 O THR A 148 54.860 6.124 −0.991 1.00 18.94 A ATOM 645 N PHE A 149 54.543 8.149 −1.916 1.00 19.16 A ATOM 646 CA PHE A 149 55.368 7.877 −3.073 1.00 18.01 A ATOM 647 CB PHE A 149 54.748 6.801 −3.989 1.00 17.23 A ATOM 648 CG PHE A 149 53.389 7.144 −4.544 1.00 16.88 A ATOM 649 CD1 PHE A 149 53.262 7.888 −5.712 1.00 18.58 A ATOM 650 CD2 PHE A 149 52.235 6.668 −3.927 1.00 17.31 A ATOM 651 CE1 PHE A 149 52.007 8.149 −6.267 1.00 19.26 A ATOM 652 CE2 PHE A 149 50.972 6.923 −4.470 1.00 19.17 A ATOM 653 CZ PHE A 149 50.858 7.663 −5.642 1.00 19.60 A ATOM 654 C PHE A 149 55.542 9.205 −3.774 1.00 20.85 A ATOM 655 O PHE A 149 54.934 10.200 −3.376 1.00 19.76 A ATOM 656 N GLN A 150 56.398 9.241 −4.782 1.00 19.79 A ATOM 657 CA GLN A 150 56.636 10.481 −5.497 1.00 24.03 A ATOM 658 CB GLN A 150 57.659 11.347 −4.739 1.00 24.45 A ATOM 659 CG GLN A 150 58.986 10.645 −4.414 1.00 26.28 A ATOM 660 CD GLN A 150 59.988 11.558 −3.692 1.00 29.02 A ATOM 661 OE1 GLN A 150 60.693 12.353 −4.321 1.00 27.05 A ATOM 662 NE2 GLN A 150 60.042 11.449 −2.365 1.00 26.47 A ATOM 663 C GLN A 150 57.160 10.203 −6.885 1.00 23.88 A ATOM 664 O GLN A 150 57.673 9.118 −7.158 1.00 24.79 A ATOM 665 N ASP A 151 56.987 11.171 −7.774 1.00 25.88 A ATOM 666 CA ASP A 151 57.527 11.047 −9.117 1.00 26.49 A ATOM 667 CB ASP A 151 56.437 11.126 −10.199 1.00 24.54 A ATOM 668 CG ASP A 151 55.544 12.336 −10.064 1.00 24.95 A ATOM 669 OD1 ASP A 151 56.005 13.379 −9.561 1.00 22.44 A ATOM 670 OD2 ASP A 151 54.369 12.242 −10.490 1.00 25.72 A ATOM 671 C ASP A 151 58.515 12.203 −9.220 1.00 28.63 A ATOM 672 O ASP A 151 58.890 12.780 −8.194 1.00 27.83 A ATOM 673 N ASP A 152 58.934 12.560 −10.426 1.00 29.21 A ATOM 674 CA ASP A 152 59.907 13.636 −10.562 1.00 31.88 A ATOM 675 CB ASP A 152 60.325 13.792 −12.026 1.00 33.94 A ATOM 676 CG ASP A 152 61.033 12.564 −12.557 1.00 38.88 A ATOM 677 OD1 ASP A 152 61.817 11.959 −11.791 1.00 39.67 A ATOM 678 OD2 ASP A 152 60.817 12.211 −13.738 1.00 41.57 A ATOM 679 C ASP A 152 59.487 14.994 −10.013 1.00 30.90 A ATOM 680 O ASP A 152 60.316 15.735 −9.482 1.00 31.69 A ATOM 681 N GLU A 153 58.207 15.322 −10.107 1.00 29.44 A ATOM 682 CA GLU A 153 57.767 16.632 −9.646 1.00 28.69 A ATOM 683 CB GLU A 153 56.984 17.327 −10.766 1.00 32.90 A ATOM 684 CG GLU A 153 57.451 16.987 −12.183 1.00 40.57 A ATOM 685 CD GLU A 153 56.920 15.643 −12.675 1.00 45.78 A ATOM 686 OE1 GLU A 153 55.682 15.482 −12.760 1.00 48.91 A ATOM 687 OE2 GLU A 153 57.736 14.747 −12.979 1.00 48.95 A ATOM 688 C GLU A 153 56.929 16.683 −8.372 1.00 26.43 A ATOM 689 O GLU A 153 56.947 17.688 −7.660 1.00 25.08 A ATOM 690 N LYS A 154 56.205 15.610 −8.069 1.00 22.39 A ATOM 691 CA LYS A 154 55.318 15.631 −6.912 1.00 21.43 A ATOM 692 CB LYS A 154 53.861 15.628 −7.398 1.00 20.33 A ATOM 693 CG LYS A 154 53.505 16.716 −8.403 1.00 21.92 A ATOM 694 CD LYS A 154 52.211 16.375 −9.146 1.00 19.70 A ATOM 695 CE LYS A 154 51.775 17.503 −10.077 1.00 20.04 A ATOM 696 NZ LYS A 154 50.631 17.094 −10.951 1.00 19.97 A ATOM 697 C LYS A 154 55.458 14.522 −5.881 1.00 20.43 A ATOM 698 O LYS A 154 55.949 13.426 −6.173 1.00 21.13 A ATOM 699 N LEU A 155 54.985 14.832 −4.676 1.00 19.69 A ATOM 700 CA LEU A 155 54.950 13.900 −3.553 1.00 19.10 A ATOM 701 CB LEU A 155 55.362 14.588 −2.252 1.00 19.65 A ATOM 702 CG LEU A 155 56.740 15.234 −2.129 1.00 21.20 A ATOM 703 CD1 LEU A 155 56.848 15.918 −0.770 1.00 23.42 A ATOM 704 CD2 LEU A 155 57.816 14.174 −2.277 1.00 23.08 A ATOM 705 C LEU A 155 53.478 13.507 −3.427 1.00 18.87 A ATOM 706 O LEU A 155 52.600 14.348 −3.620 1.00 18.61 A ATOM 707 N TYR A 156 53.209 12.249 −3.091 1.00 15.02 A ATOM 708 CA TYR A 156 51.834 11.783 −2.934 1.00 16.29 A ATOM 709 CB TYR A 156 51.470 10.769 −4.029 1.00 14.20 A ATOM 710 CG TYR A 156 51.603 11.273 −5.449 1.00 17.29 A ATOM 711 CD1 TYR A 156 52.857 11.429 −6.045 1.00 16.46 A ATOM 712 CE1 TYR A 156 52.978 11.884 −7.360 1.00 18.68 A ATOM 713 CD2 TYR A 156 50.474 11.588 −6.202 1.00 16.43 A ATOM 714 CE2 TYR A 156 50.583 12.048 −7.512 1.00 16.31 A ATOM 715 CZ TYR A 156 51.835 12.192 −8.083 1.00 18.17 A ATOM 716 OH TYR A 156 51.941 12.651 −9.371 1.00 17.47 A ATOM 717 C TYR A 156 51.657 11.108 −1.572 1.00 16.32 A ATOM 718 O TYR A 156 52.412 10.197 −1.235 1.00 16.27 A ATOM 719 N PHE A 157 50.678 11.568 −0.792 1.00 15.47 A ATOM 720 CA PHE A 157 50.385 10.966 0.508 1.00 16.66 A ATOM 721 CB PHE A 157 50.324 12.014 1.629 1.00 16.91 A ATOM 722 CG PHE A 157 51.631 12.708 1.907 1.00 18.96 A ATOM 723 CD1 PHE A 157 52.821 12.261 1.340 1.00 20.31 A ATOM 724 CD2 PHE A 157 51.664 13.829 2.732 1.00 21.12 A ATOM 725 CE1 PHE A 157 54.025 12.926 1.585 1.00 22.08 A ATOM 726 CE2 PHE A 157 52.865 14.500 2.982 1.00 22.18 A ATOM 727 CZ PHE A 157 54.045 14.045 2.405 1.00 21.27 A ATOM 728 C PHE A 157 49.016 10.308 0.404 1.00 16.52 A ATOM 729 O PHE A 157 48.029 10.979 0.110 1.00 17.32 A ATOM 730 N GLY A 158 48.953 9.002 0.644 1.00 15.97 A ATOM 731 CA GLY A 158 47.684 8.299 0.572 1.00 16.13 A ATOM 732 C GLY A 158 47.000 8.383 1.920 1.00 14.94 A ATOM 733 O GLY A 158 47.445 7.756 2.879 1.00 16.28 A ATOM 734 N LEU A 159 45.915 9.145 1.989 1.00 13.50 A ATOM 735 CA LEU A 159 45.191 9.340 3.241 1.00 15.20 A ATOM 736 CB LEU A 159 45.031 10.835 3.517 1.00 14.20 A ATOM 737 CG LEU A 159 46.270 11.726 3.385 1.00 19.00 A ATOM 738 CD1 LEU A 159 45.847 13.188 3.477 1.00 17.12 A ATOM 739 CD2 LEU A 159 47.275 11.390 4.471 1.00 14.71 A ATOM 740 C LEU A 159 43.809 8.716 3.232 1.00 15.53 A ATOM 741 O LEU A 159 43.232 8.472 2.177 1.00 16.05 A ATOM 742 N SER A 160 43.268 8.469 4.418 1.00 15.86 A ATOM 743 CA SER A 160 41.932 7.917 4.498 1.00 19.01 A ATOM 744 CB SER A 160 41.566 7.582 5.949 1.00 22.90 A ATOM 745 CG SER A 160 41.901 8.629 6.833 1.00 24.18 A ATOM 746 C SER A 160 40.987 8.968 3.924 1.00 20.43 A ATOM 747 O SER A 160 41.213 10.173 4.062 1.00 19.96 A ATOM 748 N TYR A 161 39.945 8.508 3.250 1.00 19.20 A ATOM 749 CA TYR A 161 38.975 9.406 2.644 1.00 20.37 A ATOM 750 CB TYR A 161 38.471 8.785 1.332 1.00 20.00 A ATOM 751 CG TYR A 161 37.314 9.502 0.666 1.00 20.72 A ATOM 752 CD1 TYR A 161 37.222 10.895 0.682 1.00 18.22 A ATOM 753 CE1 TYR A 161 36.180 11.557 0.029 1.00 22.24 A ATOM 754 CD2 TYR A 161 36.333 8.784 −0.020 1.00 20.53 A ATOM 755 CE2 TYR A 161 35.287 9.436 −0.678 1.00 24.24 A ATOM 756 CZ TYR A 161 35.218 10.822 −0.648 1.00 22.32 A ATOM 757 OH TYR A 161 34.194 11.471 −1.298 1.00 23.03 A ATOM 758 C TYR A 161 37.812 9.681 3.598 1.00 20.14 A ATOM 759 O TYR A 161 36.959 8.819 3.810 1.00 19.53 A ATOM 760 N ALA A 162 37.791 10.880 4.178 1.00 19.92 A ATOM 761 CA ALA A 162 36.721 11.271 5.099 1.00 21.07 A ATOM 762 CB ALA A 162 37.187 12.419 6.002 1.00 19.60 A ATOM 763 C ALA A 162 35.542 11.712 4.238 1.00 22.07 A ATOM 764 O ALA A 162 35.436 12.875 3.860 1.00 20.66 A ATOM 765 N LYS A 163 34.653 10.769 3.945 1.00 23.27 A ATOM 766 CA LYS A 163 33.503 11.017 3.080 1.00 27.12 A ATOM 767 CB LYS A 163 32.663 9.741 2.963 1.00 29.68 A ATOM 768 CG LYS A 163 33.455 8.524 2.515 1.00 37.67 A ATOM 769 CD LYS A 163 32.556 7.310 2.321 1.00 42.24 A ATOM 770 CE LYS A 163 33.373 6.034 2.185 1.00 44.48 A ATOM 771 NZ LYS A 163 34.143 5.735 3.430 1.00 44.88 A ATOM 772 C LYS A 163 32.581 12.186 3.411 1.00 25.78 A ATOM 773 O LYS A 163 32.103 12.863 2.506 1.00 26.53 A ATOM 774 N ASN A 164 32.327 12.441 4.689 1.00 24.57 A ATOM 775 CA ASN A 164 31.420 13.522 5.033 1.00 23.77 A ATOM 776 CB ASN A 164 30.610 13.129 6.265 1.00 25.02 A ATOM 777 CG ASN A 164 29.537 12.101 5.932 1.00 27.54 A ATOM 778 OD1 ASN A 164 28.772 12.281 4.983 1.00 28.79 A ATOM 779 ND2 ASN A 164 29.475 11.024 6.704 1.00 27.13 A ATOM 780 C ASN A 164 31.999 14.931 5.169 1.00 24.43 A ATOM 781 O ASN A 164 31.306 15.856 5.589 1.00 23.98 A ATOM 782 N GLY A 165 33.262 15.097 4.795 1.00 21.56 A ATOM 783 CA GLY A 165 33.873 16.414 4.836 1.00 24.39 A ATOM 784 C GLY A 165 34.191 17.043 6.181 1.00 23.62 A ATOM 785 O GLY A 165 34.380 16.352 7.177 1.00 23.26 A ATOM 786 N GLU A 166 34.234 18.373 6.186 1.00 23.22 A ATOM 787 CA GLU A 166 34.563 19.176 7.362 1.00 24.54 A ATOM 788 CB GLU A 166 35.055 20.558 6.913 1.00 25.04 A ATOM 789 CG GLU A 166 36.419 20.569 6.229 1.00 26.48 A ATOM 790 CD GLU A 166 36.699 21.889 5.517 1.00 30.02 A ATOM 791 OE1 GLU A 166 36.081 22.906 5.889 1.00 29.33 A ATOM 792 OE2 GLU A 166 37.544 21.916 4.596 1.00 30.48 A ATOM 793 C GLU A 166 33.436 19.372 8.369 1.00 24.44 A ATOM 794 O GLU A 166 32.279 19.541 8.001 1.00 22.76 A ATOM 795 N LEU A 167 33.791 19.370 9.649 1.00 22.95 A ATOM 796 CA LEU A 167 32.813 19.581 10.707 1.00 22.26 A ATOM 797 CB LEU A 167 33.497 19.481 12.073 1.00 22.32 A ATOM 798 CG LEU A 167 32.706 19.923 13.306 1.00 22.04 A ATOM 799 CD1 LEU A 167 31.454 19.074 13.463 1.00 19.66 A ATOM 800 CD2 LEU A 167 33.597 19.805 14.537 1.00 21.17 A ATOM 801 C LEU A 167 32.193 20.971 10.529 1.00 23.49 A ATOM 802 O LEU A 167 31.047 21.209 10.907 1.00 23.56 A ATOM 803 N LEU A 168 32.960 21.887 9.948 1.00 24.25 A ATOM 804 CA LEU A 168 32.473 23.245 9.722 1.00 26.64 A ATOM 805 CB LEU A 168 33.560 24.099 9.066 1.00 25.62 A ATOM 806 CG LEU A 168 33.198 25.546 8.707 1.00 27.34 A ATOM 807 CD1 LEU A 168 32.718 26.296 9.946 1.00 26.42 A ATOM 808 CD2 LEU A 168 34.418 26.238 8.119 1.00 26.74 A ATOM 809 C LEU A 168 31.234 23.218 8.829 1.00 27.13 A ATOM 810 O LEU A 168 30.297 23.989 9.030 1.00 26.01 A ATOM 811 N LYS A 169 31.233 22.320 7.848 1.00 26.41 A ATOM 812 CA LYS A 169 30.106 22.210 6.934 1.00 27.70 A ATOM 813 CB LYS A 169 30.324 21.064 5.945 1.00 30.49 A ATOM 814 CG LYS A 169 29.151 20.854 4.993 1.00 32.47 A ATOM 815 CD LYS A 169 29.407 19.728 3.998 1.00 35.98 A ATOM 816 CE LYS A 169 29.462 18.372 4.683 1.00 38.53 A ATOM 817 NZ LYS A 169 29.622 17.263 3.702 1.00 41.00 A ATOM 818 C LYS A 169 28.801 21.985 7.682 1.00 28.12 A ATOM 819 O LYS A 169 27.785 22.608 7.371 1.00 28.08 A ATOM 820 N TYR A 170 28.826 21.094 8.668 1.00 26.53 A ATOM 821 CA TYR A 170 27.624 20.791 9.434 1.00 26.95 A ATOM 822 CB TYR A 170 27.810 19.476 10.193 1.00 25.03 A ATOM 823 CG TYR A 170 27.898 18.300 9.251 1.00 26.65 A ATOM 824 CD1 TYR A 170 26.745 17.661 8.790 1.00 28.27 A ATOM 825 CE1 TYR A 170 26.814 16.642 7.839 1.00 26.85 A ATOM 826 CD2 TYR A 170 29.127 17.884 8.742 1.00 27.83 A ATOM 827 CE2 TYR A 170 29.209 16.869 7.792 1.00 27.19 A ATOM 828 CZ TYR A 170 28.049 16.254 7.343 1.00 30.02 A ATOM 829 OH TYR A 170 28.130 15.268 6.382 1.00 29.23 A ATOM 830 C TYR A 170 27.229 21.918 10.376 1.00 27.59 A ATOM 831 O TYR A 170 26.045 22.122 10.642 1.00 29.25 A ATOM 832 N ILE A 171 28.208 22.660 10.882 1.00 28.16 A ATOM 833 CA ILE A 171 27.883 23.770 11.763 1.00 29.03 A ATOM 834 CB ILE A 171 29.151 24.435 12.337 1.00 27.51 A ATOM 835 CG2 ILE A 171 28.773 25.705 13.084 1.00 27.97 A ATOM 836 CG1 ILE A 171 29.872 23.458 13.272 1.00 26.70 A ATOM 837 CD1 ILE A 171 31.163 23.996 13.856 1.00 24.07 A ATOM 838 C ILE A 171 27.094 24.796 10.944 1.00 31.41 A ATOM 839 O ILE A 171 26.088 25.335 11.407 1.00 31.69 A ATOM 840 N ARG A 172 27.546 25.047 9.719 1.00 33.21 A ATOM 841 CA ARG A 172 26.874 26.000 8.844 1.00 36.54 A ATOM 842 CB ARG A 172 27.734 26.314 7.616 1.00 37.73 A ATOM 843 CG ARG A 172 29.057 27.011 7.912 1.00 41.65 A ATOM 844 CD ARG A 172 29.708 27.492 6.616 1.00 45.29 A ATOM 845 NE ARG A 172 31.037 28.070 6.812 1.00 48.51 A ATOM 846 CZ ARG A 172 31.314 29.059 7.658 1.00 51.53 A ATOM 847 NH1 ARG A 172 30.355 29.593 8.406 1.00 53.75 A ATOM 848 NH2 ARG A 172 32.553 29.526 7.748 1.00 51.21 A ATOM 849 C ARG A 172 25.528 25.459 8.378 1.00 37.67 A ATOM 850 O ARG A 172 24.550 26.200 8.288 1.00 39.09 A ATOM 851 N LYS A 173 25.481 24.163 8.092 1.00 38.44 A ATOM 852 CA LYS A 173 24.259 23.528 7.619 1.00 39.25 A ATOM 853 CB LYS A 173 24.523 22.061 7.272 1.00 41.89 A ATOM 854 CG LYS A 173 23.279 21.298 6.830 1.00 45.52 A ATOM 855 CD LYS A 173 23.557 19.808 6.653 1.00 49.60 A ATOM 856 CE LYS A 173 24.477 19.530 5.469 1.00 52.63 A ATOM 857 NZ LYS A 173 23.855 19.894 4.160 1.00 54.61 A ATOM 858 C LYS A 173 23.089 23.608 8.595 1.00 39.30 A ATOM 859 O LYS A 173 21.981 23.960 8.201 1.00 39.62 A ATOM 860 N ILE A 174 23.320 23.282 9.863 1.00 37.96 A ATOM 861 CA ILE A 174 22.229 23.314 10.833 1.00 37.36 A ATOM 862 CB ILE A 174 22.159 21.998 11.652 1.00 37.44 A ATOM 863 CG2 ILE A 174 22.058 20.802 10.709 1.00 38.37 A ATOM 864 CG1 ILE A 174 23.397 21.850 12.532 1.00 37.25 A ATOM 865 CD1 ILE A 174 23.355 20.620 13.418 1.00 36.85 A ATOM 866 C ILE A 174 22.259 24.492 11.801 1.00 36.71 A ATOM 867 O ILE A 174 21.448 24.556 12.724 1.00 38.05 A ATOM 868 N GLY A 175 23.185 25.423 11.592 1.00 35.48 A ATOM 869 CA GLY A 175 23.265 26.585 12.462 1.00 35.29 A ATOM 870 C GLY A 175 24.053 26.360 13.737 1.00 35.06 A ATOM 871 O GLY A 175 25.066 27.019 13.970 1.00 37.46 A ATOM 872 N SER A 176 23.581 25.441 14.571 1.00 33.94 A ATOM 873 CA SER A 176 24.253 25.113 15.822 1.00 32.84 A ATOM 874 CB SER A 176 23.938 26.155 16.901 1.00 33.54 A ATOM 875 OG SER A 176 22.599 26.056 17.347 1.00 34.86 A ATOM 876 C SER A 176 23.796 23.731 16.276 1.00 32.34 A ATOM 877 O SER A 176 22.726 23.263 15.884 1.00 32.82 A ATOM 878 N PHE A 177 24.609 23.085 17.103 1.00 29.39 A ATOM 879 CA PHE A 177 24.313 21.743 17.597 1.00 27.20 A ATOM 880 CB PHE A 177 25.621 20.989 17.865 1.00 26.39 A ATOM 881 CG PHE A 177 26.372 20.585 16.622 1.00 26.18 A ATOM 882 CD1 PHE A 177 26.210 21.277 15.426 1.00 25.30 A ATOM 883 CD2 PHE A 177 27.266 19.516 16.662 1.00 26.05 A ATOM 884 CE1 PHE A 177 26.923 20.912 14.290 1.00 26.59 A ATOM 885 CE2 PHE A 177 27.986 19.143 15.532 1.00 26.06 A ATOM 886 CZ PHE A 177 27.815 19.841 14.343 1.00 25.42 A ATOM 887 C PHE A 177 23.500 21.752 18.884 1.00 27.00 A ATOM 888 O PHE A 177 23.704 22.610 19.747 1.00 26.48 A ATOM 889 N ASP A 178 22.578 20.802 19.022 1.00 26.70 A ATOM 890 CA ASP A 178 21.816 20.729 20.260 1.00 26.35 A ATOM 891 CB ASP A 178 20.621 19.773 20.142 1.00 29.90 A ATOM 892 CG ASP A 178 21.020 18.372 19.720 1.00 32.28 A ATOM 893 OD1 ASP A 178 22.157 17.949 20.014 1.00 35.21 A ATOM 894 OD2 ASP A 178 20.179 17.683 19.105 1.00 34.79 A ATOM 895 C ASP A 178 22.810 20.228 21.311 1.00 25.03 A ATOM 896 O ASP A 178 23.974 19.968 20.992 1.00 21.24 A ATOM 897 N GLU A 179 22.361 20.083 22.552 1.00 23.60 A ATOM 898 CA GLU A 179 23.247 19.644 23.619 1.00 25.18 A ATOM 899 CB GLU A 179 22.542 19.770 24.971 1.00 27.60 A ATOM 900 CG GLU A 179 23.324 19.176 26.130 1.00 32.58 A ATOM 901 CD GLU A 179 22.997 19.845 27.449 1.00 35.82 A ATOM 902 OE1 GLU A 179 21.825 20.224 27.645 1.00 35.95 A ATOM 903 OE2 GLU A 179 23.912 19.984 28.291 1.00 38.19 A ATOM 904 C GLU A 179 23.808 18.235 23.450 1.00 24.08 A ATOM 905 O GLU A 179 24.977 17.989 23.756 1.00 22.79 A ATOM 906 N THR A 180 22.983 17.316 22.961 1.00 23.36 A ATOM 907 CA THR A 180 23.412 15.935 22.761 1.00 22.15 A ATOM 908 CB THR A 180 22.224 15.054 22.320 1.00 23.77 A ATOM 909 OG1 THR A 180 21.222 15.075 23.341 1.00 26.37 A ATOM 910 CG2 THR A 180 22.670 13.616 22.088 1.00 22.66 A ATOM 911 C THR A 180 24.533 15.830 21.724 1.00 22.01 A ATOM 912 O THR A 180 25.533 15.141 21.944 1.00 19.87 A ATOM 913 N CYS A 181 24.365 16.511 20.596 1.00 21.21 A ATOM 914 CA CYS A 181 25.372 16.480 19.541 1.00 22.22 A ATOM 915 CB CYS A 181 24.800 17.065 18.250 1.00 24.62 A ATOM 916 SG CYS A 181 23.435 16.080 17.560 1.00 29.50 A ATOM 917 C CYS A 181 26.633 17.232 19.954 1.00 23.07 A ATOM 918 O CYS A 181 27.746 16.827 19.608 1.00 23.95 A ATOM 919 N THR A 182 26.463 18.325 20.695 1.00 22.76 A ATOM 920 CA THR A 182 27.606 19.103 21.161 1.00 21.49 A ATOM 921 CB THR A 182 27.167 20.346 21.978 1.00 21.37 A ATOM 922 OG1 THR A 182 26.459 21.262 21.134 1.00 22.50 A ATOM 923 CG2 THR A 182 28.379 21.046 22.565 1.00 18.36 A ATOM 924 C THR A 182 28.454 18.215 22.071 1.00 21.48 A ATOM 925 O THR A 182 29.669 18.090 21.894 1.00 19.95 A ATOM 926 N ARG A 183 27.798 17.602 23.050 1.00 18.97 A ATOM 927 CA ARG A 183 28.468 16.723 23.996 1.00 19.39 A ATOM 928 CB ARG A 183 27.455 16.140 24.984 1.00 19.46 A ATOM 929 CG ARG A 183 28.030 15.062 25.887 1.00 18.77 A ATOM 930 CD ARG A 183 27.021 14.571 26.925 1.00 21.19 A ATOM 931 NE ARG A 183 26.605 15.642 27.824 1.00 19.46 A ATOM 932 CZ ARG A 183 25.496 16.362 27.679 1.00 20.45 A ATOM 933 NH1 ARG A 183 24.672 16.123 26.666 1.00 19.81 A ATOM 934 NH2 ARG A 183 25.224 17.338 28.539 1.00 17.11 A ATOM 935 C ARG A 183 29.206 15.577 23.302 1.00 20.02 A ATOM 936 O ARG A 183 30.383 15.333 23.573 1.00 19.97 A ATOM 937 N PHE A 184 28.520 14.871 22.409 1.00 19.24 A ATOM 938 CA PHE A 184 29.144 13.746 21.722 1.00 18.04 A ATOM 939 CB PHE A 184 28.158 13.078 20.764 1.00 21.05 A ATOM 940 CG PHE A 184 28.719 11.857 20.098 1.00 22.67 A ATOM 941 CD1 PHE A 184 28.717 10.630 20.754 1.00 22.97 A ATOM 942 CD2 PHE A 184 29.317 11.949 18.850 1.00 19.97 A ATOM 943 CE1 PHE A 184 29.308 9.510 20.176 1.00 23.53 A ATOM 944 CE2 PHE A 184 29.915 10.833 18.263 1.00 24.11 A ATOM 945 CZ PHE A 184 29.910 9.613 18.928 1.00 22.97 A ATOM 946 C PHE A 184 30.403 14.127 20.941 1.00 17.99 A ATOM 947 O PHE A 184 31.461 13.531 21.130 1.00 18.89 A ATOM 948 N TYR A 185 30.292 15.110 20.056 1.00 15.73 A ATOM 949 CA TYR A 185 31.443 15.519 19.265 1.00 15.72 A ATOM 950 CB TYR A 185 30.992 16.413 18.111 1.00 17.33 A ATOM 951 CG TYR A 185 30.364 15.584 17.015 1.00 19.37 A ATOM 952 CD1 TYR A 185 31.159 14.809 16.168 1.00 16.53 A ATOM 953 CE1 TYR A 185 30.590 13.952 15.232 1.00 18.12 A ATOM 954 CD2 TYR A 185 28.976 15.484 16.892 1.00 18.18 A ATOM 955 CE2 TYR A 185 28.398 14.623 15.956 1.00 18.90 A ATOM 956 CZ TYR A 185 29.211 13.861 15.133 1.00 18.41 A ATOM 957 OH TYR A 185 28.650 12.995 14.218 1.00 20.48 A ATOM 958 C TYR A 185 32.544 16.172 20.083 1.00 15.79 A ATOM 959 O TYR A 185 33.720 16.015 19.766 1.00 17.69 A ATOM 960 N THR A 186 32.176 16.887 21.142 1.00 15.68 A ATOM 961 CA THR A 186 33.184 17.504 21.997 1.00 16.03 A ATOM 962 CB THR A 186 32.559 18.403 23.094 1.00 16.62 A ATOM 963 OG1 THR A 186 31.866 19.503 22.481 1.00 14.79 A ATOM 964 CG2 THR A 186 33.656 18.953 24.019 1.00 14.68 A ATOM 965 C THR A 186 33.954 16.375 22.680 1.00 15.59 A ATOM 966 O THR A 186 35.176 16.443 22.823 1.00 13.77 A ATOM 967 N ALA A 187 33.234 15.333 23.097 1.00 14.06 A ATOM 968 CA ALA A 187 33.869 14.196 23.757 1.00 14.74 A ATOM 969 CB ALA A 187 32.810 13.195 24.224 1.00 14.32 A ATOM 970 C ALA A 187 34.875 13.509 22.821 1.00 14.41 A ATOM 971 O ALA A 187 35.972 13.136 23.247 1.00 15.61 A ATOM 972 N GLU A 188 34.516 13.340 21.549 1.00 14.01 A ATOM 973 CA GLU A 188 35.443 12.704 20.615 1.00 13.50 A ATOM 974 CB GLU A 188 34.782 12.449 19.251 1.00 12.85 A ATOM 975 CG GLU A 188 33.622 11.454 19.282 1.00 12.71 A ATOM 976 CD GLU A 188 33.464 10.685 17.979 1.00 15.01 A ATOM 977 OE1 GLU A 188 33.687 11.275 16.899 1.00 13.21 A ATOM 978 OE2 GLU A 188 33.110 9.484 18.031 1.00 17.69 A ATOM 979 C GLU A 188 36.682 13.582 20.436 1.00 13.34 A ATOM 980 O GLU A 188 37.803 13.085 20.408 1.00 14.69 A ATOM 981 N ILE A 189 36.486 14.893 20.326 1.00 13.52 A ATOM 982 CA ILE A 189 37.627 15.787 20.159 1.00 13.35 A ATOM 983 CB ILE A 189 37.169 17.247 19.939 1.00 13.95 A ATOM 984 CG2 ILE A 189 38.381 18.165 19.822 1.00 12.47 A ATOM 985 CG1 ILE A 189 36.302 17.332 18.671 1.00 13.44 A ATOM 986 CD1 ILE A 189 35.588 18.664 18.491 1.00 14.29 A ATOM 987 C ILE A 189 38.530 15.702 21.394 1.00 14.63 A ATOM 988 O ILE A 189 39.753 15.595 21.271 1.00 12.97 A ATOM 989 N VAL A 190 37.927 15.751 22.582 1.00 14.35 A ATOM 990 CA VAL A 190 38.684 15.655 23.832 1.00 13.22 A ATOM 991 CB VAL A 190 37.743 15.690 25.061 1.00 14.28 A ATOM 992 CG1 VAL A 190 38.509 15.267 26.326 1.00 15.08 A ATOM 993 CG2 VAL A 190 37.160 17.082 25.233 1.00 12.08 A ATOM 994 C VAL A 190 39.468 14.338 23.859 1.00 14.61 A ATOM 995 O VAL A 190 40.634 14.304 24.250 1.00 13.72 A ATOM 996 N SER A 191 38.825 13.254 23.432 1.00 15.26 A ATOM 997 CA SER A 191 39.478 11.943 23.421 1.00 16.81 A ATOM 998 CB SER A 191 38.470 10.857 23.041 1.00 16.14 A ATOM 999 OG SER A 191 39.018 9.569 23.238 1.00 16.94 A ATOM 1000 C SER A 191 40.649 11.928 22.441 1.00 16.58 A ATOM 1001 O SER A 191 41.697 11.335 22.713 1.00 13.96 A ATOM 1002 N ALA A 192 40.468 12.586 21.300 1.00 15.26 A ATOM 1003 CA ALA A 192 41.518 12.645 20.292 1.00 14.37 A ATOM 1004 CB ALA A 192 40.989 13.296 19.016 1.00 14.43 A ATOM 1005 C ALA A 192 42.695 13.440 20.845 1.00 16.46 A ATOM 1006 O ALA A 192 43.851 13.038 20.697 1.00 17.96 A ATOM 1007 N LEU A 193 42.401 14.563 21.496 1.00 15.02 A ATOM 1008 CA LEU A 193 43.459 15.392 22.067 1.00 15.42 A ATOM 1009 CB LEU A 193 42.884 16.712 22.600 1.00 12.88 A ATOM 1010 CG LEU A 193 42.445 17.721 21.525 1.00 15.97 A ATOM 1011 CD1 LEU A 193 41.869 18.979 22.190 1.00 13.97 A ATOM 1012 CD2 LEU A 193 43.642 18.088 20.655 1.00 14.58 A ATOM 1013 C LEU A 193 44.211 14.659 23.174 1.00 14.49 A ATOM 1014 O LEU A 193 45.427 14.813 23.310 1.00 16.56 A ATOM 1015 N GLU A 194 43.500 13.870 23.975 1.00 13.96 A ATOM 1016 CA GLU A 194 44.179 13.123 25.032 1.00 14.08 A ATOM 1017 CB GLU A 194 43.190 12.295 25.857 1.00 14.65 A ATOM 1018 CG GLU A 194 43.882 11.301 26.789 1.00 17.09 A ATOM 1019 CD GLU A 194 42.924 10.592 27.730 1.00 19.59 A ATOM 1020 OE1 GLU A 194 41.809 10.237 27.295 1.00 19.25 A ATOM 1021 OE2 GLU A 194 43.302 10.380 28.906 1.00 20.20 A ATOM 1022 C GLU A 194 45.208 12.199 24.386 1.00 13.57 A ATOM 1023 O GLU A 194 46.337 12.093 24.847 1.00 14.23 A ATOM 1024 N TYR A 195 44.822 11.544 23.301 1.00 14.89 A ATOM 1025 CA TYR A 195 45.743 10.642 22.618 1.00 16.58 A ATOM 1026 CB TYR A 195 45.030 9.910 21.488 1.00 17.29 A ATOM 1027 CG TYR A 195 45.956 9.058 20.649 1.00 17.92 A ATOM 1028 CD1 TYR A 195 46.347 7.788 21.077 1.00 17.96 A ATOM 1029 CE1 TYR A 195 47.203 6.996 20.304 1.00 19.77 A ATOM 1030 CD2 TYR A 195 46.445 9.524 19.428 1.00 16.67 A ATOM 1031 CE2 TYR A 195 47.299 8.744 18.650 1.00 18.51 A ATOM 1032 CZ TYR A 195 47.671 7.481 19.094 1.00 20.24 A ATOM 1033 OH TYR A 195 48.506 6.705 18.325 1.00 21.89 A ATOM 1034 C TYR A 195 46.917 11.419 22.035 1.00 16.98 A ATOM 1035 O TYR A 195 48.081 11.047 22.203 1.00 14.61 A ATOM 1036 N LEU A 196 46.599 12.507 21.347 1.00 16.30 A ATOM 1037 CA LEU A 196 47.619 13.328 20.720 1.00 18.15 A ATOM 1038 CB LEU A 196 46.969 14.502 19.982 1.00 18.59 A ATOM 1039 CG LEU A 196 47.834 15.203 18.935 1.00 22.51 A ATOM 1040 CD1 LEU A 196 48.222 14.206 17.841 1.00 20.94 A ATOM 1041 CD2 LEU A 196 47.060 16.375 18.338 1.00 22.98 A ATOM 1042 C LEU A 196 48.592 13.844 21.763 1.00 17.75 A ATOM 1043 O LEU A 196 49.801 13.644 21.649 1.00 18.33 A ATOM 1044 N HIS A 197 48.064 14.495 22.792 1.00 17.12 A ATOM 1045 CA HIS A 197 48.913 15.042 23.842 1.00 18.47 A ATOM 1046 CB HIS A 197 48.069 15.866 24.817 1.00 15.90 A ATOM 1047 CG HIS A 197 47.571 17.152 24.231 1.00 19.15 A ATOM 1048 CD2 HIS A 197 47.830 17.745 23.038 1.00 18.22 A ATOM 1049 ND1 HIS A 197 46.704 17.992 24.897 1.00 17.47 A ATOM 1050 CE1 HIS A 197 46.450 19.047 24.139 1.00 19.74 A ATOM 1051 NE2 HIS A 197 47.119 18.921 23.007 1.00 15.69 A ATOM 1052 C HIS A 197 49.696 13.958 24.572 1.00 19.40 A ATOM 1053 O HIS A 197 50.823 14.192 25.021 1.00 19.42 A ATOM 1054 N GLY A 198 49.106 12.770 24.679 1.00 18.59 A ATOM 1055 CA GLY A 198 49.793 11.675 25.339 1.00 19.60 A ATOM 1056 C GLY A 198 51.075 11.307 24.612 1.00 21.86 A ATOM 1057 O GLY A 198 51.963 10.682 25.186 1.00 23.09 A ATOM 1058 N LYS A 199 51.174 11.687 23.341 1.00 22.81 A ATOM 1059 CA LYS A 199 52.368 11.401 22.549 1.00 24.43 A ATOM 1060 CB LYS A 199 51.990 10.905 21.154 1.00 26.00 A ATOM 1061 CG LYS A 199 51.378 9.520 21.133 1.00 30.98 A ATOM 1062 CD LYS A 199 51.291 9.002 19.708 1.00 36.85 A ATOM 1063 CE LYS A 199 50.832 7.559 19.682 1.00 40.37 A ATOM 1064 NZ LYS A 199 51.646 6.691 20.581 1.00 43.48 A ATOM 1065 C LYS A 199 53.253 12.631 22.414 1.00 23.88 A ATOM 1066 O LYS A 199 54.144 12.669 21.568 1.00 24.97 A ATOM 1067 N GLY A 200 52.997 13.638 23.243 1.00 24.00 A ATOM 1068 CA GLY A 200 53.790 14.853 23.203 1.00 22.12 A ATOM 1069 C GLY A 200 53.665 15.632 21.907 1.00 22.14 A ATOM 1070 O GLY A 200 54.632 16.231 21.439 1.00 22.41 A ATOM 1071 N ILE A 201 52.475 15.630 21.320 1.00 20.00 A ATOM 1072 CA ILE A 201 52.252 16.355 20.080 1.00 18.93 A ATOM 1073 CB ILE A 201 51.784 15.414 18.955 1.00 19.70 A ATOM 1074 CG2 ILE A 201 51.414 16.226 17.716 1.00 20.12 A ATOM 1075 CG1 ILE A 201 52.880 14.395 18.636 1.00 20.03 A ATOM 1076 CD1 ILE A 201 52.408 13.258 17.745 1.00 22.75 A ATOM 1077 C ILE A 201 51.193 17.425 20.270 1.00 19.87 A ATOM 1078 O ILE A 201 50.121 17.161 20.817 1.00 20.08 A ATOM 1079 N ILE A 202 51.508 18.633 19.815 1.00 19.94 A ATOM 1080 CA ILE A 202 50.601 19.772 19.891 1.00 20.45 A ATOM 1081 CB ILE A 202 51.352 21.040 20.356 1.00 22.21 A ATOM 1082 CG2 ILE A 202 50.381 22.220 20.470 1.00 22.67 A ATOM 1083 CG1 ILE A 202 52.033 20.775 21.700 1.00 24.19 A ATOM 1084 CD1 ILE A 202 52.914 21.920 22.169 1.00 25.39 A ATOM 1085 C ILE A 202 50.105 19.999 18.464 1.00 20.71 A ATOM 1086 O ILE A 202 50.910 20.067 17.538 1.00 19.48 A ATOM 1087 N HIS A 203 48.795 20.108 18.270 1.00 18.65 A ATOM 1088 CA HIS A 203 48.280 20.319 16.919 1.00 18.02 A ATOM 1089 CB HIS A 203 46.775 20.057 16.874 1.00 16.31 A ATOM 1090 CG HIS A 203 46.199 20.136 15.495 1.00 18.36 A ATOM 1091 CD2 HIS A 203 46.043 21.186 14.655 1.00 16.42 A ATOM 1092 ND1 HIS A 203 45.759 19.026 14.806 1.00 19.50 A ATOM 1093 CE1 HIS A 203 45.359 19.389 13.600 1.00 17.64 A ATOM 1094 NE2 HIS A 203 45.522 20.694 13.483 1.00 20.87 A ATOM 1095 C HIS A 203 48.589 21.738 16.405 1.00 18.92 A ATOM 1096 O HIS A 203 49.073 21.906 15.282 1.00 16.21 A ATOM 1097 N ARG A 204 48.301 22.744 17.232 1.00 18.60 A ATOM 1098 CA ARG A 204 48.552 24.157 16.914 1.00 19.81 A ATOM 1099 CB ARG A 204 49.998 24.365 16.458 1.00 21.61 A ATOM 1100 CG ARG A 204 51.024 24.137 17.550 1.00 23.82 A ATOM 1101 CD ARG A 204 52.323 24.870 17.252 1.00 27.62 A ATOM 1102 NE ARG A 204 52.932 24.449 15.994 1.00 29.43 A ATOM 1103 CZ ARG A 204 54.125 24.861 15.572 1.00 33.10 A ATOM 1104 NH1 ARG A 204 54.835 25.706 16.311 1.00 32.12 A ATOM 1105 NH2 ARG A 204 54.614 24.426 14.418 1.00 30.25 A ATOM 1106 C ARG A 204 47.624 24.830 15.905 1.00 20.03 A ATOM 1107 O ARG A 204 47.711 26.038 15.698 1.00 20.88 A ATOM 1108 N ASP A 205 46.755 24.071 15.255 1.00 18.96 A ATOM 1109 CA ASP A 205 45.828 24.692 14.325 1.00 17.90 A ATOM 1110 CB ASP A 205 46.418 24.741 12.914 1.00 18.95 A ATOM 1111 CG ASP A 205 45.655 25.688 12.008 1.00 20.36 A ATOM 1112 OD1 ASP A 205 44.939 26.560 12.545 1.00 20.35 A ATOM 1113 OD2 ASP A 205 45.772 25.573 10.771 1.00 22.49 A ATOM 1114 C ASP A 205 44.500 23.956 14.328 1.00 19.60 A ATOM 1115 O ASP A 205 43.876 23.751 13.287 1.00 21.53 A ATOM 1116 N LEU A 206 44.063 23.569 15.521 1.00 18.53 A ATOM 1117 CA LEU A 206 42.813 22.851 15.667 1.00 19.18 A ATOM 1118 CB LEU A 206 42.693 22.295 17.087 1.00 18.94 A ATOM 1119 CG LEU A 206 41.511 21.358 17.346 1.00 23.10 A ATOM 1120 CD1 LEU A 206 41.615 20.142 16.436 1.00 23.01 A ATOM 1121 CD2 LEU A 206 41.504 20.933 18.808 1.00 22.97 A ATOM 1122 C LEU A 206 41.639 23.772 15.361 1.00 19.05 A ATOM 1123 O LEU A 206 41.556 24.880 15.886 1.00 19.25 A ATOM 1124 N LYS A 207 40.740 23.307 14.500 1.00 17.54 A ATOM 1125 CA LYS A 207 39.564 24.081 14.110 1.00 18.60 A ATOM 1126 CB LYS A 207 39.980 25.248 13.196 1.00 18.98 A ATOM 1127 CG LYS A 207 40.786 24.817 11.982 1.00 18.20 A ATOM 1128 CD LYS A 207 41.246 26.000 11.139 1.00 21.42 A ATOM 1129 CE LYS A 207 42.223 25.537 10.062 1.00 23.21 A ATOM 1130 NZ LYS A 207 42.561 26.604 9.084 1.00 29.61 A ATOM 1131 C LYS A 207 38.566 23.181 13.388 1.00 18.18 A ATOM 1132 O LYS A 207 38.921 22.100 12.915 1.00 18.11 A ATOM 1133 N PRO A 208 37.298 23.614 13.293 1.00 20.26 A ATOM 1134 CD PRO A 208 36.713 24.833 13.882 1.00 18.79 A ATOM 1135 CA PRO A 208 36.272 22.814 12.616 1.00 19.67 A ATOM 1136 CB PRO A 208 35.063 23.742 12.608 1.00 19.45 A ATOM 1137 CG PRO A 208 35.231 24.509 13.891 1.00 21.81 A ATOM 1138 C PRO A 208 36.674 22.372 11.209 1.00 21.04 A ATOM 1139 O PRO A 208 36.264 21.307 10.751 1.00 21.19 A ATOM 1140 N GLU A 209 37.474 23.188 10.528 1.00 21.69 A ATOM 1141 CA GLU A 209 37.928 22.872 9.170 1.00 22.64 A ATOM 1142 CB GLU A 209 38.644 24.084 8.558 1.00 23.65 A ATOM 1143 CG GLU A 209 39.253 23.825 7.185 1.00 27.24 A ATOM 1144 CD GLU A 209 40.155 24.958 6.716 1.00 29.40 A ATOM 1145 OE1 GLU A 209 39.660 26.094 6.553 1.00 29.68 A ATOM 1146 OE2 GLU A 209 41.363 24.711 6.511 1.00 30.07 A ATOM 1147 C GLU A 209 38.879 21.668 9.159 1.00 22.28 A ATOM 1148 O GLU A 209 38.955 20.933 8.170 1.00 21.36 A ATOM 1149 N ASN A 210 39.600 21.490 10.263 1.00 19.90 A ATOM 1150 CA ASN A 210 40.574 20.412 10.436 1.00 19.44 A ATOM 1151 CB ASN A 210 41.744 20.912 11.287 1.00 20.07 A ATOM 1152 CG ASN A 210 42.746 21.698 10.479 1.00 25.77 A ATOM 1153 OD1 ASN A 210 43.571 22.427 11.029 1.00 26.73 A ATOM 1154 ND2 ASN A 210 42.687 21.548 9.158 1.00 25.15 A ATOM 1155 C ASN A 210 40.005 19.151 11.078 1.00 18.63 A ATOM 1156 O ASN A 210 40.712 18.154 11.234 1.00 18.29 A ATOM 1157 N ILE A 211 38.739 19.202 11.469 1.00 16.31 A ATOM 1158 CA ILE A 211 38.090 18.058 12.085 1.00 15.49 A ATOM 1159 CB ILE A 211 37.336 18.488 13.354 1.00 15.40 A ATOM 1160 CG2 ILE A 211 36.582 17.311 13.950 1.00 14.59 A ATOM 1161 CG1 ILE A 211 38.342 19.046 14.365 1.00 15.91 A ATOM 1162 CD1 ILE A 211 37.720 19.669 15.590 1.00 15.98 A ATOM 1163 C ILE A 211 37.131 17.485 11.059 1.00 17.26 A ATOM 1164 O ILE A 211 35.995 17.947 10.926 1.00 18.16 A ATOM 1165 N LEU A 212 37.599 16.486 10.317 1.00 15.97 A ATOM 1166 CA LEU A 212 36.784 15.875 9.274 1.00 17.08 A ATOM 1167 CB LEU A 212 37.685 15.249 8.202 1.00 17.78 A ATOM 1168 CG LEU A 212 38.785 16.157 7.640 1.00 18.92 A ATOM 1169 CD1 LEU A 212 39.476 15.450 6.485 1.00 22.09 A ATOM 1170 CD2 LEU A 212 38.188 17.482 7.166 1.00 19.91 A ATOM 1171 C LEU A 212 35.843 14.825 9.837 1.00 18.35 A ATOM 1172 O LEU A 212 35.957 14.433 11.002 1.00 19.39 A ATOM 1173 N LEU A 213 34.915 14.368 9.000 1.00 17.84 A ATOM 1174 CA LEU A 213 33.942 13.362 9.403 1.00 19.94 A ATOM 1175 CB LEU A 213 32.556 14.004 9.487 1.00 20.84 A ATOM 1176 CG LEU A 213 32.396 15.059 10.583 1.00 20.31 A ATOM 1177 CD1 LEU A 213 31.124 15.837 10.367 1.00 22.75 A ATOM 1178 CD2 LEU A 213 32.379 14.378 11.940 1.00 23.93 A ATOM 1179 C LEU A 213 33.914 12.187 8.426 1.00 20.98 A ATOM 1180 O LEU A 213 33.743 12.379 7.218 1.00 19.55 A ATOM 1181 N ASN A 214 34.088 10.970 8.935 1.00 20.44 A ATOM 1182 CA ASN A 214 34.055 9.814 8.049 1.00 23.77 A ATOM 1183 CB ASN A 214 34.745 8.596 8.674 1.00 25.30 A ATOM 1184 CG ASN A 214 34.077 8.127 9.948 1.00 32.04 A ATOM 1185 OD1 ASN A 214 32.908 8.422 10.206 1.00 34.43 A ATOM 1186 ND2 ASN A 214 34.818 7.369 10.752 1.00 33.85 A ATOM 1187 C ASN A 214 32.618 9.466 7.693 1.00 24.07 A ATOM 1188 O ASN A 214 31.672 10.113 8.150 1.00 19.94 A ATOM 1189 N GLU A 215 32.459 8.433 6.879 1.00 25.77 A ATOM 1190 CA GLU A 215 31.138 8.003 6.445 1.00 28.69 A ATOM 1191 CB GLU A 215 31.275 6.796 5.513 1.00 31.98 A ATOM 1192 CG GLU A 215 29.970 6.334 4.896 1.00 40.22 A ATOM 1193 CD GLU A 215 30.182 5.312 3.795 1.00 44.27 A ATOM 1194 OE1 GLU A 215 30.817 4.268 4.065 1.00 46.46 A ATOM 1195 OE2 GLU A 215 29.716 5.556 2.660 1.00 46.13 A ATOM 1196 C GLU A 215 30.188 7.673 7.601 1.00 28.41 A ATOM 1197 O GLU A 215 28.971 7.769 7.447 1.00 28.52 A ATOM 1198 N ASP A 216 30.737 7.287 8.752 1.00 26.77 A ATOM 1199 CA ASP A 216 29.914 6.953 9.917 1.00 27.28 A ATOM 1200 CB ASP A 216 30.538 5.795 10.696 1.00 31.27 A ATOM 1201 CG ASP A 216 30.390 4.466 9.979 1.00 37.61 A ATOM 1202 OD1 ASP A 216 29.274 4.170 9.499 1.00 39.45 A ATOM 1203 OD2 ASP A 216 31.382 3.710 9.902 1.00 41.84 A ATOM 1204 C ASP A 216 29.697 8.135 10.862 1.00 26.37 A ATOM 1205 O ASP A 216 29.136 7.984 11.950 1.00 25.73 A ATOM 1206 N MET A 217 30.156 9.306 10.441 1.00 23.02 A ATOM 1207 CA MET A 217 30.015 10.527 11.218 1.00 21.83 A ATOM 1208 CB MET A 217 28.537 10.789 11.517 1.00 23.24 A ATOM 1209 CG MET A 217 27.742 11.186 10.274 1.00 22.98 A ATOM 1210 SD MET A 217 28.464 12.616 9.430 1.00 27.57 A ATOM 1211 CE MET A 217 27.679 13.974 10.332 1.00 26.68 A ATOM 1212 C MET A 217 30.844 10.618 12.502 1.00 21.51 A ATOM 1213 O MET A 217 30.474 11.323 13.440 1.00 18.62 A ATOM 1214 N HIS A 218 31.957 9.892 12.544 1.00 20.10 A ATOM 1215 CA HIS A 218 32.873 9.964 13.678 1.00 19.86 A ATOM 1216 CB HIS A 218 33.482 8.594 13.977 1.00 20.21 A ATOM 1217 CG HIS A 218 32.551 7.667 14.698 1.00 22.40 A ATOM 1218 CD2 HIS A 218 31.910 6.547 14.287 1.00 21.27 A ATOM 1219 ND1 HIS A 218 32.177 7.863 16.011 1.00 19.59 A ATOM 1220 CE1 HIS A 218 31.348 6.902 16.379 1.00 21.88 A ATOM 1221 NE2 HIS A 218 31.168 6.091 15.351 1.00 22.08 A ATOM 1222 C HIS A 218 33.947 10.921 13.172 1.00 19.10 A ATOM 1223 O HIS A 218 34.170 11.004 11.965 1.00 20.31 A ATOM 1224 N ILE A 219 34.617 11.638 14.067 1.00 17.21 A ATOM 1225 CA ILE A 219 35.628 12.586 13.618 1.00 15.26 A ATOM 1226 CB ILE A 219 35.987 13.614 14.716 1.00 15.38 A ATOM 1227 CG2 ILE A 219 34.722 14.305 15.221 1.00 14.58 A ATOM 1228 CG1 ILE A 219 36.734 12.919 15.864 1.00 14.46 A ATOM 1229 CD1 ILE A 219 37.279 13.885 16.911 1.00 13.74 A ATOM 1230 C ILE A 219 36.929 11.944 13.161 1.00 16.21 A ATOM 1231 O ILE A 219 37.238 10.799 13.500 1.00 15.88 A ATOM 1232 N GLN A 220 37.677 12.711 12.378 1.00 15.62 A ATOM 1233 CA GLN A 220 38.980 12.316 11.876 1.00 17.84 A ATOM 1234 CB GLN A 220 38.872 11.595 10.525 1.00 20.00 A ATOM 1235 CG GLN A 220 38.463 10.129 10.659 1.00 26.97 A ATOM 1236 CD GLN A 220 38.648 9.343 9.372 1.00 29.95 A ATOM 1237 OE1 GLN A 220 37.968 9.590 8.373 1.00 33.12 A ATOM 1238 NE2 GLN A 220 39.578 8.393 9.389 1.00 30.47 A ATOM 1239 C GLN A 220 39.757 13.610 11.735 1.00 17.00 A ATOM 1240 O GLN A 220 39.609 14.339 10.751 1.00 18.27 A ATOM 1241 N ILE A 221 40.566 13.906 12.746 1.00 14.34 A ATOM 1242 CA ILE A 221 41.361 15.120 12.753 1.00 14.46 A ATOM 1243 CB ILE A 221 41.867 15.416 14.175 1.00 12.30 A ATOM 1244 CG2 ILE A 221 42.764 16.656 14.167 1.00 14.78 A ATOM 1245 CG1 ILE A 221 40.660 15.613 15.102 1.00 13.92 A ATOM 1246 CD1 ILE A 221 41.003 15.901 16.543 1.00 15.06 A ATOM 1247 C ILE A 221 42.536 14.996 11.783 1.00 15.44 A ATOM 1248 O ILE A 221 43.106 13.915 11.613 1.00 13.93 A ATOM 1249 N THR A 222 42.877 16.101 11.127 1.00 15.36 A ATOM 1250 CA THR A 222 43.980 16.098 10.174 1.00 17.52 A ATOM 1251 CB THR A 222 43.470 15.836 8.750 1.00 19.92 A ATOM 1252 OG1 THR A 222 44.587 15.637 7.875 1.00 18.78 A ATOM 1253 CG2 THR A 222 42.630 17.018 8.257 1.00 18.16 A ATOM 1254 C THR A 222 44.735 17.428 10.192 1.00 19.60 A ATOM 1255 O THR A 222 44.509 18.257 11.084 1.00 18.59 A ATOM 1256 N ASP A 223 45.630 17.610 9.216 1.00 18.69 A ATOM 1257 CA ASP A 223 46.440 18.825 9.069 1.00 20.12 A ATOM 1258 CB ASP A 223 45.532 20.065 9.108 1.00 23.51 A ATOM 1259 CG ASP A 223 46.248 21.335 8.670 1.00 27.09 A ATOM 1260 OD1 ASP A 223 47.283 21.227 7.975 1.00 26.28 A ATOM 1261 OD2 ASP A 223 45.765 22.438 9.009 1.00 26.15 A ATOM 1262 C ASP A 223 47.516 18.913 10.150 1.00 21.73 A ATOM 1263 O ASP A 223 47.439 19.751 11.055 1.00 22.76 A ATOM 1264 N PHE A 224 48.535 18.063 10.027 1.00 20.75 A ATOM 1265 CA PHE A 224 49.611 17.988 11.009 1.00 20.11 A ATOM 1266 CB PHE A 224 49.805 16.527 11.424 1.00 20.62 A ATOM 1267 CG PHE A 224 48.682 15.991 12.263 1.00 21.41 A ATOM 1268 CD1 PHE A 224 48.598 16.312 13.614 1.00 23.05 A ATOM 1269 CD2 PHE A 224 47.681 15.212 11.693 1.00 22.27 A ATOM 1270 CE1 PHE A 224 47.528 15.868 14.389 1.00 23.30 A ATOM 1271 CE2 PHE A 224 46.606 14.763 12.457 1.00 21.11 A ATOM 1272 CZ PHE A 224 46.530 15.093 13.807 1.00 22.02 A ATOM 1273 C PHE A 224 50.957 18.583 10.619 1.00 20.45 A ATOM 1274 O PHE A 224 51.905 18.547 11.407 1.00 20.73 A ATOM 1275 N GLY A 225 51.049 19.125 9.412 1.00 22.02 A ATOM 1276 CA GLY A 225 52.301 19.713 8.981 1.00 22.66 A ATOM 1277 C GLY A 225 52.742 20.822 9.920 1.00 24.99 A ATOM 1278 O GLY A 225 53.939 21.041 10.122 1.00 24.52 A ATOM 1279 N THR A 226 51.779 21.524 10.508 1.00 23.50 A ATOM 1280 CA THR A 226 52.106 22.613 11.416 1.00 25.16 A ATOM 1281 CB THR A 226 51.199 23.829 11.160 1.00 24.76 A ATOM 1282 OG1 THR A 226 49.831 23.410 11.113 1.00 22.68 A ATOM 1283 CG2 THR A 226 51.571 24.490 9.834 1.00 25.00 A ATOM 1284 C THR A 226 52.046 22.233 12.894 1.00 25.79 A ATOM 1285 O THR A 226 52.019 23.100 13.768 1.00 24.54 A ATOM 1286 N ALA A 227 52.037 20.935 13.173 1.00 24.97 A ATOM 1287 CA ALA A 227 52.004 20.475 14.550 1.00 25.49 A ATOM 1288 CB ALA A 227 51.659 18.993 14.607 1.00 22.85 A ATOM 1289 C ALA A 227 53.384 20.715 15.149 1.00 27.70 A ATOM 1290 O ALA A 227 54.331 21.047 14.435 1.00 26.60 A ATOM 1291 N LYS A 228 53.491 20.558 16.461 1.00 28.53 A ATOM 1292 CA LYS A 228 54.760 20.745 17.149 1.00 32.12 A ATOM 1293 CB LYS A 228 54.699 21.974 18.054 1.00 33.81 A ATOM 1294 CG LYS A 228 56.007 22.294 18.765 1.00 41.23 A ATOM 1295 CD LYS A 228 57.082 22.725 17.768 1.00 47.57 A ATOM 1296 CE LYS A 228 58.401 23.056 18.462 1.00 49.82 A ATOM 1297 NZ LYS A 228 59.459 23.425 17.480 1.00 51.49 A ATOM 1298 C LYS A 228 55.019 19.504 17.985 1.00 33.25 A ATOM 1299 O LYS A 228 54.190 19.129 18.815 1.00 33.70 A ATOM 1300 N VAL A 229 56.159 18.860 17.756 1.00 33.64 A ATOM 1301 CA VAL A 229 56.516 17.661 18.501 1.00 34.66 A ATOM 1302 CB VAL A 229 57.248 16.646 17.609 1.00 33.50 A ATOM 1303 CG1 VAL A 229 57.619 15.419 18.415 1.00 32.34 A ATOM 1304 CG2 VAL A 229 56.370 16.264 16.436 1.00 34.25 A ATOM 1305 C VAL A 229 57.420 18.035 19.668 1.00 37.57 A ATOM 1306 O VAL A 229 58.581 18.392 19.474 1.00 35.91 A ATOM 1307 N LEU A 230 56.877 17.948 20.878 1.00 40.57 A ATOM 1308 CA LEU A 230 57.615 18.289 22.088 1.00 46.10 A ATOM 1309 CB LEU A 230 56.654 18.417 23.270 1.00 44.71 A ATOM 1310 CG LEU A 230 55.627 19.545 23.207 1.00 44.50 A ATOM 1311 CD1 LEU A 230 54.673 19.430 24.383 1.00 44.39 A ATOM 1312 CD2 LEU A 230 56.340 20.885 23.214 1.00 44.81 A ATOM 1313 C LEU A 230 58.695 17.279 22.440 1.00 50.42 A ATOM 1314 O LEU A 230 58.603 16.104 22.089 1.00 51.64 A ATOM 1315 N SER A 231 59.717 17.756 23.145 1.00 55.81 A ATOM 1316 CA SER A 231 60.824 16.914 23.583 1.00 61.14 A ATOM 1317 CB SER A 231 62.077 17.200 22.750 1.00 61.27 A ATOM 1318 OG SER A 231 62.444 18.568 22.823 1.00 62.85 A ATOM 1319 C SER A 231 61.124 17.126 25.071 1.00 64.65 A ATOM 1320 O SER A 231 61.392 16.164 25.794 1.00 65.70 A ATOM 1321 N PRO A 232 61.081 18.387 25.549 1.00 67.54 A ATOM 1322 CD PRO A 232 60.854 19.651 24.823 1.00 68.60 A ATOM 1323 CA PRO A 232 61.358 18.655 26.966 1.00 68.74 A ATOM 1324 CB PRO A 232 61.109 20.158 27.086 1.00 68.83 A ATOM 1325 CG PRO A 232 61.505 20.666 25.737 1.00 68.96 A ATOM 1326 C PRO A 232 60.460 17.846 27.899 1.00 69.17 A ATOM 1327 O PRO A 232 59.335 17.494 27.541 1.00 69.94 A ATOM 1328 N ALA A 237 57.424 23.198 27.637 1.00 80.06 A ATOM 1329 CA ALA A 237 56.783 23.047 26.335 1.00 79.29 A ATOM 1330 CB ALA A 237 55.275 22.907 26.512 1.00 78.64 A ATOM 1331 C ALA A 237 57.092 24.239 25.433 1.00 79.07 A ATOM 1332 O ALA A 237 56.250 25.113 25.249 1.00 79.47 A ATOM 1333 N ALA A 238 58.297 24.280 24.871 1.00 78.57 A ATOM 1334 CA ALA A 238 58.683 25.383 23.992 1.00 78.50 A ATOM 1335 CB ALA A 238 60.186 25.347 23.728 1.00 78.50 A ATOM 1336 C ALA A 238 57.920 25.327 22.673 1.00 78.15 A ATOM 1337 O ALA A 238 57.243 24.341 22.375 1.00 77.96 A ATOM 1338 N ALA A 239 58.027 26.393 21.887 1.00 77.28 A ATOM 1339 CA ALA A 239 57.338 26.452 20.603 1.00 76.27 A ATOM 1340 CB ALA A 239 55.849 26.489 20.827 1.00 76.61 A ATOM 1341 C ALA A 239 57.766 27.667 19.793 1.00 75.38 A ATOM 1342 O ALA A 239 58.955 27.955 19.700 1.00 75.89 A ATOM 1343 N ASN A 240 56.781 28.357 19.214 1.00 73.95 A ATOM 1344 CA ASN A 240 56.967 29.553 18.389 1.00 71.07 A ATOM 1345 CB ASN A 240 58.151 30.400 18.874 1.00 71.47 A ATOM 1346 CG ASN A 240 59.459 30.055 18.174 1.00 72.06 A ATOM 1347 OD1 ASN A 240 59.575 30.149 16.943 1.00 72.03 A ATOM 1348 ND2 ASN A 240 60.470 29.665 18.964 1.00 71.91 A ATOM 1349 C ASN A 240 57.188 29.178 16.928 1.00 69.41 A ATOM 1350 O ASN A 240 57.480 28.024 16.624 1.00 70.09 A ATOM 1351 N ALA A 241 57.055 30.165 16.038 1.00 66.62 A ATOM 1352 CA ALA A 241 57.246 30.013 14.585 1.00 63.94 A ATOM 1353 C ALA A 241 55.952 30.080 13.772 1.00 60.63 A ATOM 1354 O ALA A 241 55.840 30.880 12.845 1.00 61.29 A ATOM 1355 CB ALA A 241 57.979 28.704 14.246 1.00 65.23 A ATOM 1356 N PHE A 242 54.984 29.236 14.113 1.00 56.72 A ATOM 1357 CA PHE A 242 53.712 29.196 13.394 1.00 52.53 A ATOM 1358 CB PHE A 242 53.419 27.767 12.923 1.00 49.14 A ATOM 1359 CG PHE A 242 52.040 27.590 12.354 1.00 47.38 A ATOM 1360 CD1 PHE A 242 51.731 28.067 11.085 1.00 47.69 A ATOM 1361 CD2 PHE A 242 51.038 26.975 13.102 1.00 45.45 A ATOM 1362 CE1 PHE A 242 50.445 27.937 10.565 1.00 46.75 A ATOM 1363 CE2 PHE A 242 49.751 26.840 12.594 1.00 45.41 A ATOM 1364 CZ PHE A 242 49.453 27.323 11.322 1.00 46.55 A ATOM 1365 C PHE A 242 52.534 29.688 14.229 1.00 50.08 A ATOM 1366 O PHE A 242 52.502 29.505 15.444 1.00 49.86 A ATOM 1367 N VAL A 243 51.566 30.305 13.557 1.00 47.67 A ATOM 1368 CA VAL A 243 50.355 30.809 14.200 1.00 46.21 A ATOM 1369 CB VAL A 243 50.340 32.352 14.258 1.00 47.36 A ATOM 1370 CG1 VAL A 243 49.012 32.844 14.825 1.00 47.54 A ATOM 1371 CG2 VAL A 243 51.497 32.842 15.109 1.00 48.50 A ATOM 1372 C VAL A 243 49.150 30.342 13.389 1.00 44.12 A ATOM 1373 O VAL A 243 48.956 30.765 12.247 1.00 44.46 A ATOM 1374 N GLY A 244 48.348 29.467 13.985 1.00 40.48 A ATOM 1375 CA GLY A 244 47.176 28.941 13.306 1.00 37.65 A ATOM 1376 C GLY A 244 46.101 29.960 12.964 1.00 35.39 A ATOM 1377 O GLY A 244 46.313 31.168 13.065 1.00 35.92 A ATOM 1378 N THR A 245 44.936 29.463 12.560 1.00 33.30 A ATOM 1379 CA THR A 245 43.813 30.312 12.184 1.00 30.20 A ATOM 1380 CB THR A 245 42.593 29.450 11.829 1.00 32.00 A ATOM 1381 OG1 THR A 245 42.952 28.573 10.755 1.00 32.81 A ATOM 1382 CG2 THR A 245 41.419 30.319 11.390 1.00 28.34 A ATOM 1383 C THR A 245 43.476 31.296 13.296 1.00 27.96 A ATOM 1384 O THR A 245 43.212 30.907 14.434 1.00 25.46 A ATOM 1385 N ALA A 246 43.486 32.576 12.938 1.00 25.22 A ATOM 1386 CA ALA A 246 43.247 33.675 13.867 1.00 23.27 A ATOM 1387 CB ALA A 246 42.956 34.955 13.082 1.00 22.94 A ATOM 1388 C ALA A 246 42.178 33.475 14.934 1.00 21.27 A ATOM 1389 O ALA A 246 42.431 33.705 16.114 1.00 20.93 A ATOM 1390 N GLN A 247 40.988 33.047 14.536 1.00 19.67 A ATOM 1391 CA GLN A 247 39.911 32.886 15.504 1.00 20.17 A ATOM 1392 CB GLN A 247 38.608 32.535 14.779 1.00 21.89 A ATOM 1393 CG GLN A 247 38.522 33.076 13.355 1.00 26.18 A ATOM 1394 CD GLN A 247 37.220 33.794 13.064 1.00 27.30 A ATOM 1395 OE1 GLN A 247 36.172 33.447 13.605 1.00 30.13 A ATOM 1396 NE2 GLN A 247 37.278 34.792 12.189 1.00 28.70 A ATOM 1397 C GLN A 247 40.181 31.849 16.595 1.00 19.43 A ATOM 1398 O GLN A 247 39.546 31.883 17.648 1.00 18.93 A ATOM 1399 N TYR A 248 41.132 30.948 16.359 1.00 18.60 A ATOM 1400 CA TYR A 248 41.441 29.896 17.329 1.00 19.20 A ATOM 1401 CB TYR A 248 41.333 28.529 16.642 1.00 17.53 A ATOM 1402 CG TYR A 248 40.013 28.362 15.927 1.00 19.32 A ATOM 1403 CD1 TYR A 248 38.859 28.010 16.625 1.00 17.69 A ATOM 1404 CE1 TYR A 248 37.617 27.976 15.990 1.00 18.18 A ATOM 1405 CD2 TYR A 248 39.897 28.664 14.569 1.00 16.87 A ATOM 1406 CE2 TYR A 248 38.665 28.635 13.924 1.00 19.17 A ATOM 1407 CZ TYR A 248 37.527 28.295 14.643 1.00 19.46 A ATOM 1408 OH TYR A 248 36.299 28.311 14.023 1.00 18.98 A ATOM 1409 C TYR A 248 42.810 30.039 17.993 1.00 20.42 A ATOM 1410 O TYR A 248 43.208 29.191 18.792 1.00 19.19 A ATOM 1411 N VAL A 249 43.523 31.114 17.673 1.00 20.20 A ATOM 1412 CA VAL A 249 44.841 31.343 18.251 1.00 20.91 A ATOM 1413 CB VAL A 249 45.542 32.532 17.570 1.00 21.18 A ATOM 1414 CG1 VAL A 249 46.821 32.896 18.317 1.00 22.45 A ATOM 1415 CG2 VAL A 249 45.862 32.170 16.139 1.00 24.01 A ATOM 1416 C VAL A 249 44.764 31.606 19.750 1.00 21.52 A ATOM 1417 O VAL A 249 43.915 32.368 20.216 1.00 22.72 A ATOM 1418 N SER A 250 45.654 30.965 20.503 1.00 20.70 A ATOM 1419 CA SER A 250 45.697 31.133 21.951 1.00 21.65 A ATOM 1420 CB SER A 250 46.370 29.919 22.613 1.00 22.02 A ATOM 1421 OG SER A 250 47.692 29.725 22.132 1.00 22.12 A ATOM 1422 C SER A 250 46.476 32.402 22.280 1.00 22.13 A ATOM 1423 O SER A 250 47.332 32.828 21.511 1.00 22.77 A ATOM 1424 N PRO A 251 46.180 33.029 23.425 1.00 22.23 A ATOM 1425 CD PRO A 251 45.163 32.684 24.433 1.00 22.97 A ATOM 1426 CA PRO A 251 46.893 34.254 23.800 1.00 22.52 A ATOM 1427 CB PRO A 251 46.233 34.650 25.127 1.00 23.06 A ATOM 1428 CG PRO A 251 45.726 33.329 25.676 1.00 22.55 A ATOM 1429 C PRO A 251 48.414 34.115 23.907 1.00 22.15 A ATOM 1430 O PRO A 251 49.143 35.047 23.563 1.00 22.62 A ATOM 1431 N GLU A 252 48.901 32.966 24.367 1.00 20.69 A ATOM 1432 CA GLU A 252 50.347 32.772 24.500 1.00 21.40 A ATOM 1433 CB GLU A 252 50.673 31.382 25.071 1.00 20.59 A ATOM 1434 CG GLU A 252 49.993 30.232 24.352 1.00 21.91 A ATOM 1435 CD GLU A 252 48.691 29.822 25.014 1.00 21.51 A ATOM 1436 OE1 GLU A 252 47.989 30.707 25.550 1.00 21.46 A ATOM 1437 OE2 GLU A 252 48.367 28.613 24.993 1.00 20.23 A ATOM 1438 C GLU A 252 51.071 32.970 23.167 1.00 22.99 A ATOM 1439 O GLU A 252 52.191 33.480 23.136 1.00 23.17 A ATOM 1440 N LEU A 253 50.441 32.576 22.064 1.00 23.00 A ATOM 1441 CA LEU A 253 51.068 32.753 20.758 1.00 25.62 A ATOM 1442 CB LEU A 253 50.277 32.029 19.669 1.00 26.75 A ATOM 1443 CG LEU A 253 50.743 30.620 19.296 1.00 31.87 A ATOM 1444 CD1 LEU A 253 50.433 29.651 20.422 1.00 31.81 A ATOM 1445 CD2 LEU A 253 50.044 30.179 18.015 1.00 31.86 A ATOM 1446 C LEU A 253 51.201 34.228 20.371 1.00 26.94 A ATOM 1447 O LEU A 253 52.107 34.601 19.626 1.00 27.09 A ATOM 1448 N LEU A 254 50.297 35.059 20.877 1.00 25.83 A ATOM 1449 CA LEU A 254 50.297 36.485 20.564 1.00 27.26 A ATOM 1450 CB LEU A 254 48.858 37.006 20.564 1.00 25.84 A ATOM 1451 CG LEU A 254 47.882 36.290 19.621 1.00 24.69 A ATOM 1452 CD1 LEU A 254 46.459 36.724 19.932 1.00 23.64 A ATOM 1453 CD2 LEU A 254 48.236 36.597 18.177 1.00 24.24 A ATOM 1454 C LEU A 254 51.134 37.314 21.537 1.00 30.62 A ATOM 1455 O LEU A 254 51.633 38.383 21.187 1.00 32.35 A ATOM 1456 N THR A 255 51.292 36.821 22.758 1.00 32.47 A ATOM 1457 CA THR A 255 52.056 37.547 23.759 1.00 36.70 A ATOM 1458 CB THR A 255 51.368 37.478 25.127 1.00 34.51 A ATOM 1459 OG1 THR A 255 51.188 36.106 25.494 1.00 35.49 A ATOM 1460 CG2 THR A 255 50.013 38.166 25.077 1.00 33.40 A ATOM 1461 C THR A 255 53.477 37.035 23.910 1.00 40.09 A ATOM 1462 O THR A 255 54.430 37.793 23.772 1.00 43.69 A ATOM 1463 N GLU A 256 53.617 35.747 24.189 1.00 44.77 A ATOM 1464 CA GLU A 256 54.932 35.144 24.382 1.00 49.15 A ATOM 1465 CB GLU A 256 54.866 34.143 25.534 1.00 51.24 A ATOM 1466 CG GLU A 256 54.514 34.786 26.862 1.00 56.03 A ATOM 1467 CD GLU A 256 54.053 33.780 27.893 1.00 58.83 A ATOM 1468 OE1 GLU A 256 54.766 32.776 28.107 1.00 62.13 A ATOM 1469 OE2 GLU A 256 52.979 33.996 28.494 1.00 60.34 A ATOM 1470 C GLU A 256 55.475 34.456 23.137 1.00 50.09 A ATOM 1471 O GLU A 256 56.616 33.995 23.127 1.00 50.42 A ATOM 1472 N LYS A 257 54.658 34.389 22.090 1.00 51.21 A ATOM 1473 CA LYS A 257 55.064 33.746 20.845 1.00 51.22 A ATOM 1474 CB LYS A 257 56.244 34.502 20.227 1.00 53.28 A ATOM 1475 CG LYS A 257 56.558 34.125 18.790 1.00 55.19 A ATOM 1476 CD LYS A 257 57.709 34.961 18.253 1.00 57.52 A ATOM 1477 CE LYS A 257 57.952 34.694 16.777 1.00 58.52 A ATOM 1478 NZ LYS A 257 58.290 33.268 16.515 1.00 60.88 A ATOM 1479 C LYS A 257 55.467 32.302 21.138 1.00 50.74 A ATOM 1480 O LYS A 257 56.432 31.790 20.577 1.00 52.26 A ATOM 1481 N SER A 258 54.721 31.654 22.027 1.00 48.07 A ATOM 1482 CA SER A 258 54.999 30.273 22.402 1.00 46.87 A ATOM 1483 CB SER A 258 55.590 30.229 23.812 1.00 48.88 A ATOM 1484 OG SER A 258 54.741 30.892 24.734 1.00 53.14 A ATOM 1485 C SER A 258 53.735 29.415 22.342 1.00 44.07 A ATOM 1486 O SER A 258 52.617 29.932 22.417 1.00 44.17 A ATOM 1487 N ALA A 259 53.917 28.105 22.204 1.00 38.30 A ATOM 1488 CA ALA A 259 52.793 27.180 22.127 1.00 34.73 A ATOM 1489 CB ALA A 259 52.551 26.779 20.684 1.00 34.16 A ATOM 1490 C ALA A 259 53.042 25.940 22.977 1.00 32.34 A ATOM 1491 O ALA A 259 54.172 25.459 23.086 1.00 31.81 A ATOM 1492 N CYS A 260 51.975 25.428 23.579 1.00 28.58 A ATOM 1493 CA CYS A 260 52.056 24.244 24.425 1.00 26.27 A ATOM 1494 CB CYS A 260 52.183 24.654 25.892 1.00 26.53 A ATOM 1495 SG CYS A 260 50.846 25.739 26.469 1.00 32.91 A ATOM 1496 C CYS A 260 50.786 23.435 24.224 1.00 22.83 A ATOM 1497 O CYS A 260 49.892 23.856 23.495 1.00 22.14 A ATOM 1498 N LYS A 261 50.706 22.277 24.868 1.00 20.02 A ATOM 1499 CA LYS A 261 49.526 21.434 24.744 1.00 20.65 A ATOM 1500 CB LYS A 261 49.619 20.243 25.696 1.00 23.28 A ATOM 1501 CG LYS A 261 50.716 19.253 25.347 1.00 27.44 A ATOM 1502 CD LYS A 261 50.732 18.117 26.350 1.00 29.98 A ATOM 1503 CE LYS A 261 51.922 17.203 26.134 1.00 32.34 A ATOM 1504 NZ LYS A 261 51.940 16.121 27.153 1.00 33.28 A ATOM 1505 C LYS A 261 48.268 22.229 25.062 1.00 19.20 A ATOM 1506 O LYS A 261 47.253 22.092 24.387 1.00 18.08 A ATOM 1507 N SER A 262 48.358 23.068 26.089 1.00 16.92 A ATOM 1508 CA SER A 262 47.235 23.883 26.534 1.00 18.13 A ATOM 1509 CB SER A 262 47.644 24.698 27.770 1.00 18.27 A ATOM 1510 OG SER A 262 46.517 25.258 28.421 1.00 22.53 A ATOM 1511 C SER A 262 46.736 24.811 25.424 1.00 16.77 A ATOM 1512 O SER A 262 45.591 25.254 25.450 1.00 15.69 A ATOM 1513 N SER A 263 47.595 25.118 24.456 1.00 16.44 A ATOM 1514 CA SER A 263 47.175 25.970 23.347 1.00 16.89 A ATOM 1515 CB SER A 263 48.340 26.228 22.382 1.00 18.49 A ATOM 1516 OG SER A 263 49.402 26.909 23.031 1.00 22.10 A ATOM 1517 C SER A 263 46.040 25.257 22.612 1.00 17.79 A ATOM 1518 O SER A 263 45.099 25.898 22.148 1.00 17.57 A ATOM 1519 N ASP A 264 46.119 23.928 22.517 1.00 16.30 A ATOM 1520 CA ASP A 264 45.069 23.166 21.836 1.00 16.72 A ATOM 1521 CB ASP A 264 45.483 21.704 21.620 1.00 15.92 A ATOM 1522 CG ASP A 264 46.544 21.539 20.548 1.00 17.93 A ATOM 1523 OD1 ASP A 264 46.642 22.412 19.661 1.00 16.78 A ATOM 1524 OD2 ASP A 264 47.265 20.515 20.579 1.00 16.64 A ATOM 1525 C ASP A 264 43.773 23.194 22.646 1.00 17.67 A ATOM 1526 O ASP A 264 42.681 23.197 22.076 1.00 18.27 A ATOM 1527 N LEU A 265 43.898 23.205 23.974 1.00 15.49 A ATOM 1528 CA LEU A 265 42.730 23.232 24.849 1.00 14.75 A ATOM 1529 CB LEU A 265 43.147 23.038 26.313 1.00 11.38 A ATOM 1530 CG LEU A 265 43.711 21.641 26.621 1.00 14.04 A ATOM 1531 CD1 LEU A 265 44.249 21.579 28.052 1.00 13.96 A ATOM 1532 CD2 LEU A 265 42.619 20.603 26.416 1.00 11.62 A ATOM 1533 C LEU A 265 41.999 24.557 24.675 1.00 15.13 A ATOM 1534 O LEU A 265 40.777 24.620 24.785 1.00 16.75 A ATOM 1535 N TRP A 266 42.746 25.622 24.405 1.00 16.08 A ATOM 1536 CA TRP A 266 42.118 26.918 24.184 1.00 16.96 A ATOM 1537 CB TRP A 266 43.176 28.015 24.023 1.00 17.28 A ATOM 1538 CG TRP A 266 42.618 29.326 23.521 1.00 20.54 A ATOM 1539 CD2 TRP A 266 42.313 30.490 24.301 1.00 20.07 A ATOM 1540 CE2 TRP A 266 41.782 31.459 23.417 1.00 20.46 A ATOM 1541 CE3 TRP A 266 42.435 30.810 25.660 1.00 20.68 A ATOM 1542 CD1 TRP A 266 42.270 29.631 22.231 1.00 19.53 A ATOM 1543 NE1 TRP A 266 41.769 30.908 22.163 1.00 19.61 A ATOM 1544 CZ2 TRP A 266 41.372 32.727 23.850 1.00 20.90 A ATOM 1545 CZ3 TRP A 266 42.026 32.073 26.091 1.00 19.45 A ATOM 1546 CH2 TRP A 266 41.501 33.015 25.185 1.00 20.71 A ATOM 1547 C TRP A 266 41.284 26.795 22.913 1.00 17.22 A ATOM 1548 O TRP A 266 40.139 27.240 22.863 1.00 18.03 A ATOM 1549 N ALA A 267 41.863 26.181 21.886 1.00 17.50 A ATOM 1550 CA ALA A 267 41.155 25.990 20.626 1.00 16.16 A ATOM 1551 CB ALA A 267 42.050 25.290 19.621 1.00 14.28 A ATOM 1552 C ALA A 267 39.901 25.159 20.891 1.00 16.28 A ATOM 1553 O ALA A 267 38.835 25.436 20.346 1.00 16.46 A ATOM 1554 N LEU A 268 40.031 24.144 21.739 1.00 16.57 A ATOM 1555 CA LEU A 268 38.890 23.299 22.084 1.00 17.03 A ATOM 1556 CB LEU A 268 39.292 22.260 23.139 1.00 15.35 A ATOM 1557 CG LEU A 268 38.158 21.429 23.754 1.00 19.00 A ATOM 1558 CD1 LEU A 268 37.505 20.578 22.678 1.00 16.17 A ATOM 1559 CD2 LEU A 268 38.718 20.537 24.881 1.00 17.49 A ATOM 1560 C LEU A 268 37.766 24.179 22.628 1.00 15.72 A ATOM 1561 O LEU A 268 36.603 24.031 22.247 1.00 15.28 A ATOM 1562 N GLY A 269 38.119 25.099 23.520 1.00 14.34 A ATOM 1563 CA GLY A 269 37.124 25.989 24.092 1.00 13.39 A ATOM 1564 C GLY A 269 36.406 26.808 23.031 1.00 14.94 A ATOM 1565 O GLY A 269 35.193 27.014 23.114 1.00 14.76 A ATOM 1566 N CYS A 270 37.146 27.279 22.030 1.00 13.86 A ATOM 1567 CA CYS A 270 36.539 28.061 20.958 1.00 16.80 A ATOM 1568 CB CYS A 270 37.611 28.634 20.023 1.00 15.97 A ATOM 1569 SG CYS A 270 38.751 29.810 20.780 1.00 20.48 A ATOM 1570 C CYS A 270 35.598 27.175 20.140 1.00 17.50 A ATOM 1571 O CYS A 270 34.516 27.604 19.741 1.00 18.38 A ATOM 1572 N ILE A 271 36.022 25.939 19.887 1.00 16.99 A ATOM 1573 CA ILE A 271 35.221 25.004 19.104 1.00 16.66 A ATOM 1574 CB ILE A 271 36.038 23.741 18.778 1.00 16.53 A ATOM 1575 CG2 ILE A 271 35.155 22.694 18.102 1.00 16.34 A ATOM 1576 CG1 ILE A 271 37.222 24.129 17.882 1.00 15.59 A ATOM 1577 CD1 ILE A 271 38.239 23.018 17.690 1.00 14.88 A ATOM 1578 C ILE A 271 33.920 24.626 19.809 1.00 16.74 A ATOM 1579 O ILE A 271 32.865 24.576 19.179 1.00 17.12 A ATOM 1580 N ILE A 272 33.990 24.357 21.111 1.00 16.13 A ATOM 1581 CA ILE A 272 32.785 24.021 21.862 1.00 18.30 A ATOM 1582 CB ILE A 272 33.097 23.747 23.346 1.00 17.77 A ATOM 1583 CG2 ILE A 272 31.796 23.666 24.152 1.00 17.96 A ATOM 1584 CG1 ILE A 272 33.877 22.437 23.481 1.00 19.55 A ATOM 1585 CD1 ILE A 272 34.446 22.217 24.886 1.00 18.64 A ATOM 1586 C ILE A 272 31.824 25.207 21.776 1.00 19.51 A ATOM 1587 O ILE A 272 30.624 25.037 21.554 1.00 20.44 A ATOM 1588 N TYR A 273 32.362 26.409 21.947 1.00 18.52 A ATOM 1589 CA TYR A 273 31.553 27.615 21.881 1.00 20.48 A ATOM 1590 CB TYR A 273 32.418 28.847 22.162 1.00 18.98 A ATOM 1591 CG TYR A 273 31.663 30.161 22.125 1.00 20.26 A ATOM 1592 CD1 TYR A 273 31.229 30.709 20.916 1.00 20.67 A ATOM 1593 CE1 TYR A 273 30.536 31.917 20.880 1.00 20.98 A ATOM 1594 CD2 TYR A 273 31.383 30.857 23.302 1.00 19.82 A ATOM 1595 CE2 TYR A 273 30.691 32.062 23.280 1.00 20.62 A ATOM 1596 CZ TYR A 273 30.271 32.587 22.067 1.00 21.15 A ATOM 1597 OH TYR A 273 29.588 33.776 22.049 1.00 21.86 A ATOM 1598 C TYR A 273 30.902 27.730 20.507 1.00 21.54 A ATOM 1599 O TYR A 273 29.719 28.049 20.401 1.00 22.80 A ATOM 1600 N GLN A 274 31.676 27.454 19.461 1.00 21.05 A ATOM 1601 CA GLN A 274 31.176 27.538 18.095 1.00 21.48 A ATOM 1602 CB GLN A 274 32.323 27.341 17.097 1.00 21.41 A ATOM 1603 CG GLN A 274 31.934 27.596 15.645 1.00 23.15 A ATOM 1604 CD GLN A 274 33.131 27.588 14.706 1.00 24.80 A ATOM 1605 OE1 GLN A 274 34.276 27.446 15.139 1.00 22.51 A ATOM 1606 NE2 GLN A 274 32.870 27.750 13.413 1.00 22.96 A ATOM 1607 C GLN A 274 30.076 26.517 17.828 1.00 21.51 A ATOM 1608 O GLN A 274 29.123 26.806 17.108 1.00 20.50 A ATOM 1609 N LEU A 275 30.207 25.324 18.403 1.00 21.44 A ATOM 1610 CA LEU A 275 29.196 24.282 18.208 1.00 20.95 A ATOM 1611 CB LEU A 275 29.645 22.958 18.846 1.00 19.11 A ATOM 1612 CG LEU A 275 30.775 22.182 18.159 1.00 21.43 A ATOM 1613 CD1 LEU A 275 31.118 20.936 18.963 1.00 17.64 A ATOM 1614 CD2 LEU A 275 30.342 21.795 16.754 1.00 20.34 A ATOM 1615 C LEU A 275 27.860 24.697 18.815 1.00 21.32 A ATOM 1616 O LEU A 275 26.802 24.461 18.229 1.00 19.75 A ATOM 1617 N VAL A 276 27.921 25.322 19.987 1.00 19.10 A ATOM 1618 CA VAL A 276 26.724 25.750 20.702 1.00 22.47 A ATOM 1619 CB VAL A 276 27.011 25.882 22.217 1.00 20.87 A ATOM 1620 CG1 VAL A 276 25.742 26.291 22.957 1.00 19.68 A ATOM 1621 CG2 VAL A 276 27.550 24.558 22.766 1.00 19.43 A ATOM 1622 C VAL A 276 26.127 27.075 20.211 1.00 23.89 A ATOM 1623 O VAL A 276 24.910 27.199 20.070 1.00 24.90 A ATOM 1624 N ALA A 277 26.983 28.062 19.965 1.00 24.56 A ATOM 1625 CA ALA A 277 26.533 29.374 19.518 1.00 24.72 A ATOM 1626 CB ALA A 277 27.504 30.444 19.999 1.00 24.36 A ATOM 1627 C ALA A 277 26.378 29.458 18.005 1.00 25.76 A ATOM 1628 O ALA A 277 25.577 30.242 17.502 1.00 26.39 A ATOM 1629 N GLY A 278 27.142 28.651 17.280 1.00 25.13 A ATOM 1630 CA GLY A 278 27.062 28.673 15.834 1.00 25.58 A ATOM 1631 C GLY A 278 28.163 29.524 15.231 1.00 26.50 A ATOM 1632 O GLY A 278 28.374 29.510 14.015 1.00 28.17 A ATOM 1633 N LEU A 279 28.866 30.262 16.086 1.00 24.44 A ATOM 1634 CA LEU A 279 29.962 31.130 15.656 1.00 25.21 A ATOM 1635 CB LEU A 279 29.468 32.575 15.500 1.00 25.78 A ATOM 1636 CG LEU A 279 28.364 32.899 14.490 1.00 28.17 A ATOM 1637 CD1 LEU A 279 27.922 34.344 14.684 1.00 26.60 A ATOM 1638 CD2 LEU A 279 28.862 32.670 13.071 1.00 26.52 A ATOM 1639 C LEU A 279 31.093 31.116 16.687 1.00 23.47 A ATOM 1640 O LEU A 279 30.848 30.994 17.882 1.00 24.44 A ATOM 1641 N PRO A 280 32.349 31.239 16.236 1.00 23.35 A ATOM 1642 CD PRO A 280 32.831 31.404 14.855 1.00 22.26 A ATOM 1643 CA PRO A 280 33.464 31.239 17.189 1.00 23.81 A ATOM 1644 CB PRO A 280 34.692 31.293 16.282 1.00 23.24 A ATOM 1645 CG PRO A 280 34.189 32.020 15.073 1.00 24.89 A ATOM 1646 C PRO A 280 33.353 32.444 18.137 1.00 22.69 A ATOM 1647 O PRO A 280 32.750 33.457 17.788 1.00 22.11 A ATOM 1648 N PRO A 281 33.939 32.344 19.345 1.00 23.06 A ATOM 1649 CD PRO A 281 34.810 31.223 19.734 1.00 21.37 A ATOM 1650 CA PRO A 281 33.935 33.375 20.395 1.00 23.67 A ATOM 1651 CB PRO A 281 34.781 32.751 21.509 1.00 24.89 A ATOM 1652 CG PRO A 281 34.749 31.287 21.219 1.00 25.24 A ATOM 1653 C PRO A 281 34.481 34.752 20.017 1.00 23.75 A ATOM 1654 O PRO A 281 33.869 35.781 20.317 1.00 21.02 A ATOM 1655 N PHE A 282 35.644 34.763 19.379 1.00 22.17 A ATOM 1656 CA PHE A 282 36.293 36.007 18.998 1.00 23.16 A ATOM 1657 CB PHE A 282 37.765 35.943 19.406 1.00 21.01 A ATOM 1658 CG PHE A 282 37.975 35.482 20.822 1.00 22.66 A ATOM 1659 CD1 PHE A 282 37.806 36.361 21.888 1.00 20.06 A ATOM 1660 CD2 PHE A 282 38.291 34.151 21.093 1.00 20.72 A ATOM 1661 CE1 PHE A 282 37.947 35.921 23.206 1.00 22.66 A ATOM 1662 CE2 PHE A 282 38.433 33.702 22.405 1.00 20.97 A ATOM 1663 CZ PHE A 282 38.261 34.590 23.466 1.00 19.58 A ATOM 1664 C PHE A 282 36.169 36.263 17.503 1.00 24.39 A ATOM 1665 O PHE A 282 36.802 35.585 16.694 1.00 25.80 A ATOM 1666 N ARG A 283 35.355 37.248 17.142 1.00 24.99 A ATOM 1667 CA ARG A 283 35.141 37.594 15.741 1.00 26.33 A ATOM 1668 CB ARG A 283 33.721 37.209 15.316 1.00 28.91 A ATOM 1669 CG ARG A 283 33.293 35.808 15.724 1.00 30.27 A ATOM 1670 CD ARG A 283 31.904 35.493 15.188 1.00 33.36 A ATOM 1671 NE ARG A 283 30.890 36.392 15.733 1.00 32.76 A ATOM 1672 CZ ARG A 283 30.372 36.287 16.952 1.00 34.79 A ATOM 1673 NH1 ARG A 283 30.767 35.317 17.768 1.00 35.77 A ATOM 1674 NH2 ARG A 283 29.458 37.156 17.359 1.00 36.12 A ATOM 1675 C ARG A 283 35.328 39.096 15.544 1.00 26.47 A ATOM 1676 O ARG A 283 35.029 39.888 16.438 1.00 26.28 A ATOM 1677 N ALA A 284 35.818 39.486 14.373 1.00 26.70 A ATOM 1678 CA ALA A 284 36.033 40.899 14.079 1.00 27.84 A ATOM 1679 CB ALA A 284 37.188 41.442 14.914 1.00 26.24 A ATOM 1680 C ALA A 284 36.327 41.077 12.602 1.00 28.35 A ATOM 1681 O ALA A 284 36.560 40.101 11.891 1.00 29.91 A ATOM 1682 N GLY A 285 36.332 42.329 12.153 1.00 29.29 A ATOM 1683 CA GLY A 285 36.577 42.631 10.753 1.00 29.52 A ATOM 1684 C GLY A 285 37.893 42.156 10.168 1.00 30.12 A ATOM 1685 O GLY A 285 37.974 41.862 8.976 1.00 30.60 A ATOM 1686 N ASN A 286 38.939 42.097 10.983 1.00 28.49 A ATOM 1687 CA ASN A 286 40.231 41.644 10.489 1.00 26.71 A ATOM 1688 CB ASN A 286 41.050 42.825 9.945 1.00 26.11 A ATOM 1689 CG ASN A 286 41.310 43.900 10.990 1.00 27.83 A ATOM 1690 OD1 ASN A 286 41.877 43.631 12.049 1.00 27.84 A ATOM 1691 ND2 ASN A 286 40.908 45.131 10.685 1.00 25.95 A ATOM 1692 C ASN A 286 40.997 40.924 11.584 1.00 26.03 A ATOM 1693 O ASN A 286 40.540 40.851 12.723 1.00 25.66 A ATOM 1694 N GLU A 287 42.162 40.391 11.239 1.00 24.81 A ATOM 1695 CA GLU A 287 42.965 39.662 12.206 1.00 27.59 A ATOM 1696 CB GLU A 287 44.145 38.985 11.510 1.00 30.17 A ATOM 1697 CG GLU A 287 43.776 37.632 10.931 1.00 38.21 A ATOM 1698 CD GLU A 287 44.900 36.998 10.140 1.00 41.86 A ATOM 1699 OE1 GLU A 287 46.061 37.036 10.608 1.00 43.08 A ATOM 1700 OE2 GLU A 287 44.612 36.449 9.052 1.00 45.22 A ATOM 1701 C GLU A 287 43.459 40.485 13.383 1.00 25.05 A ATOM 1702 O GLU A 287 43.382 40.030 14.521 1.00 26.41 A ATOM 1703 N TYR A 288 43.966 41.685 13.122 1.00 23.04 A ATOM 1704 CA TYR A 288 44.460 42.528 14.205 1.00 22.34 A ATOM 1705 CB TYR A 288 44.867 43.913 13.691 1.00 21.07 A ATOM 1706 CG TYR A 288 45.275 44.858 14.805 1.00 21.07 A ATOM 1707 CD1 TYR A 288 46.533 44.762 15.405 1.00 21.23 A ATOM 1708 CE1 TYR A 288 46.891 45.588 16.475 1.00 20.43 A ATOM 1709 CD2 TYR A 288 44.380 45.809 15.302 1.00 22.32 A ATOM 1710 CE2 TYR A 288 44.725 46.637 16.373 1.00 23.28 A ATOM 1711 CZ TYR A 288 45.981 46.518 16.953 1.00 22.96 A ATOM 1712 OH TYR A 288 46.316 47.313 18.024 1.00 23.18 A ATOM 1713 C TYR A 288 43.402 42.698 15.288 1.00 21.38 A ATOM 1714 O TYR A 288 43.710 42.616 16.473 1.00 22.09 A ATOM 1715 N LEU A 289 42.159 42.939 14.874 1.00 21.88 A ATOM 1716 CA LEU A 289 41.055 43.130 15.811 1.00 21.98 A ATOM 1717 CB LEU A 289 39.821 43.673 15.078 1.00 22.90 A ATOM 1718 CG LEU A 289 39.896 45.130 14.601 1.00 26.52 A ATOM 1719 CD1 LEU A 289 38.706 45.436 13.696 1.00 26.55 A ATOM 1720 CD2 LEU A 289 39.914 46.071 15.807 1.00 23.13 A ATOM 1721 C LEU A 289 40.686 41.849 16.560 1.00 21.24 A ATOM 1722 O LEU A 289 40.256 41.897 17.715 1.00 20.72 A ATOM 1723 N ILE A 290 40.843 40.708 15.900 1.00 19.62 A ATOM 1724 CA ILE A 290 40.538 39.433 16.533 1.00 18.54 A ATOM 1725 CB ILE A 290 40.560 38.281 15.509 1.00 18.52 A ATOM 1726 CG2 ILE A 290 40.503 36.934 16.234 1.00 17.63 A ATOM 1727 CG1 ILE A 290 39.378 38.429 14.545 1.00 18.88 A ATOM 1728 CD1 ILE A 290 39.421 37.483 13.357 1.00 19.81 A ATOM 1729 C ILE A 290 41.578 39.167 17.618 1.00 19.09 A ATOM 1730 O ILE A 290 41.236 38.788 18.737 1.00 18.20 A ATOM 1731 N PHE A 291 42.849 39.376 17.286 1.00 18.76 A ATOM 1732 CA PHE A 291 43.925 39.156 18.247 1.00 20.75 A ATOM 1733 CB PHE A 291 45.286 39.434 17.606 1.00 20.71 A ATOM 1734 CG PHE A 291 45.644 38.480 16.503 1.00 22.92 A ATOM 1735 CD1 PHE A 291 45.065 37.214 16.443 1.00 22.98 A ATOM 1736 CD2 PHE A 291 46.588 38.830 15.543 1.00 22.91 A ATOM 1737 CE1 PHE A 291 45.423 36.310 15.440 1.00 24.51 A ATOM 1738 CE2 PHE A 291 46.954 37.931 14.535 1.00 25.54 A ATOM 1739 CZ PHE A 291 46.370 36.670 14.485 1.00 23.29 A ATOM 1740 C PHE A 291 43.739 40.061 19.451 1.00 21.72 A ATOM 1741 O PHE A 291 43.992 39.671 20.593 1.00 22.32 A ATOM 1742 N GLN A 292 43.284 41.275 19.178 1.00 23.27 A ATOM 1743 CA GLN A 292 43.055 42.264 20.216 1.00 24.01 A ATOM 1744 CB GLN A 292 42.574 43.559 19.562 1.00 25.77 A ATOM 1745 CG GLN A 292 42.577 44.773 20.447 1.00 28.45 A ATOM 1746 CD GLN A 292 42.469 46.057 19.638 1.00 29.83 A ATOM 1747 OE1 GLN A 292 41.520 46.244 18.872 1.00 27.16 A ATOM 1748 NE2 GLN A 292 43.449 46.944 19.799 1.00 27.61 A ATOM 1749 C GLN A 292 42.018 41.733 21.204 1.00 22.97 A ATOM 1750 O GLN A 292 42.200 41.832 22.415 1.00 21.64 A ATOM 1751 N LYS A 293 40.937 41.154 20.687 1.00 21.82 A ATOM 1752 CA LYS A 293 39.895 40.612 21.558 1.00 22.18 A ATOM 1753 CB LYS A 293 38.664 40.223 20.740 1.00 22.69 A ATOM 1754 CG LYS A 293 37.919 41.407 20.153 1.00 25.78 A ATOM 1755 CD LYS A 293 36.651 40.961 19.429 1.00 27.88 A ATOM 1756 CE LYS A 293 35.857 42.161 18.926 1.00 30.85 A ATOM 1757 NZ LYS A 293 34.612 41.750 18.214 1.00 32.98 A ATOM 1758 C LYS A 293 40.398 39.398 22.343 1.00 21.20 A ATOM 1759 O LYS A 293 40.041 39.204 23.509 1.00 22.01 A ATOM 1760 N ILE A 294 41.226 38.583 21.702 1.00 19.91 A ATOM 1761 CA ILE A 294 41.774 37.394 22.347 1.00 20.28 A ATOM 1762 CB ILE A 294 42.631 36.575 21.349 1.00 18.98 A ATOM 1763 CG2 ILE A 294 43.481 35.550 22.098 1.00 17.70 A ATOM 1764 CG1 ILE A 294 41.716 35.897 20.318 1.00 17.93 A ATOM 1765 CD1 ILE A 294 42.467 35.237 19.178 1.00 16.21 A ATOM 1766 C ILE A 294 42.618 37.727 23.587 1.00 21.94 A ATOM 1767 O ILE A 294 42.366 37.199 24.673 1.00 20.86 A ATOM 1768 N ILE A 295 43.610 38.600 23.439 1.00 21.88 A ATOM 1769 CA ILE A 295 44.461 38.934 24.582 1.00 24.25 A ATOM 1770 CB ILE A 295 45.668 39.805 24.175 1.00 23.93 A ATOM 1771 CG2 ILE A 295 46.514 39.066 23.140 1.00 24.61 A ATOM 1772 CG1 ILE A 295 45.189 41.151 23.637 1.00 24.58 A ATOM 1773 CD1 ILE A 295 46.317 42.149 23.433 1.00 26.69 A ATOM 1774 C ILE A 295 43.720 39.636 25.717 1.00 24.80 A ATOM 1775 O ILE A 295 44.214 39.687 26.842 1.00 24.76 A ATOM 1776 N LYS A 296 42.539 40.173 25.425 1.00 25.33 A ATOM 1777 CA LYS A 296 41.743 40.853 26.444 1.00 26.80 A ATOM 1778 CB LYS A 296 41.178 42.170 25.894 1.00 27.39 A ATOM 1779 CG LYS A 296 42.240 43.141 25.413 1.00 31.79 A ATOM 1780 CD LYS A 296 41.634 44.410 24.826 1.00 35.56 A ATOM 1781 CE LYS A 296 41.009 45.283 25.900 1.00 39.29 A ATOM 1782 NZ LYS A 296 40.564 46.603 25.357 1.00 41.72 A ATOM 1783 C LYS A 296 40.593 39.958 26.893 1.00 25.50 A ATOM 1784 O LYS A 296 39.770 40.361 27.713 1.00 24.02 A ATOM 1785 N LEU A 297 40.550 38.742 26.349 1.00 25.67 A ATOM 1786 CA LEU A 297 39.500 37.777 26.666 1.00 25.16 A ATOM 1787 CB LEU A 297 39.632 37.285 28.111 1.00 24.80 A ATOM 1788 CG LEU A 297 38.766 36.068 28.460 1.00 26.43 A ATOM 1789 CD1 LEU A 297 39.238 34.852 27.646 1.00 26.70 A ATOM 1790 CD2 LEU A 297 38.856 35.777 29.951 1.00 24.84 A ATOM 1791 C LEU A 297 38.151 38.459 26.467 1.00 25.11 A ATOM 1792 O LEU A 297 37.261 38.378 27.309 1.00 25.28 A ATOM 1793 N GLU A 298 38.007 39.127 25.331 1.00 24.98 A ATOM 1794 CA GLU A 298 36.786 39.847 25.023 1.00 25.31 A ATOM 1795 CB GLU A 298 37.143 41.139 24.291 1.00 27.13 A ATOM 1796 CG GLU A 298 35.991 42.092 24.108 1.00 31.28 A ATOM 1797 CD GLU A 298 36.419 43.362 23.410 1.00 34.40 A ATOM 1798 OE1 GLU A 298 37.348 44.027 23.918 1.00 35.90 A ATOM 1799 OE2 GLU A 298 35.832 43.693 22.359 1.00 36.16 A ATOM 1800 C GLU A 298 35.766 39.057 24.207 1.00 23.79 A ATOM 1801 O GLU A 298 35.832 39.017 22.979 1.00 24.35 A ATOM 1802 N TYR A 299 34.825 38.427 24.902 1.00 23.45 A ATOM 1803 CA TYR A 299 33.760 37.663 24.265 1.00 23.98 A ATOM 1804 CB TYR A 299 34.264 36.304 23.755 1.00 20.13 A ATOM 1805 CG TYR A 299 34.348 35.233 24.828 1.00 21.17 A ATOM 1806 CD1 TYR A 299 35.336 35.279 25.810 1.00 19.32 A ATOM 1807 CE1 TYR A 299 35.389 34.332 26.826 1.00 19.30 A ATOM 1808 CD2 TYR A 299 33.410 34.201 24.888 1.00 18.96 A ATOM 1809 CE2 TYR A 299 33.456 33.243 25.907 1.00 19.41 A ATOM 1810 CZ TYR A 299 34.449 33.321 26.870 1.00 18.79 A ATOM 1811 OH TYR A 299 34.511 32.401 27.881 1.00 18.77 A ATOM 1812 C TYR A 299 32.699 37.437 25.331 1.00 25.20 A ATOM 1813 O TYR A 299 32.942 37.681 26.506 1.00 26.46 A ATOM 1814 N ASP A 300 31.522 36.981 24.927 1.00 26.94 A ATOM 1815 CA ASP A 300 30.467 36.710 25.891 1.00 30.60 A ATOM 1816 CB ASP A 300 29.665 37.981 26.179 1.00 35.86 A ATOM 1817 CG ASP A 300 29.228 38.687 24.923 1.00 42.04 A ATOM 1818 OD1 ASP A 300 28.450 38.088 24.149 1.00 45.98 A ATOM 1819 OD2 ASP A 300 29.666 39.840 24.707 1.00 45.69 A ATOM 1820 C ASP A 300 29.564 35.608 25.363 1.00 29.26 A ATOM 1821 O ASP A 300 29.590 35.299 24.172 1.00 28.64 A ATOM 1822 N PHE A 301 28.778 35.011 26.253 1.00 28.96 A ATOM 1823 CA PHE A 301 27.884 33.924 25.871 1.00 30.48 A ATOM 1824 CB PHE A 301 27.818 32.854 26.968 1.00 29.17 A ATOM 1825 CG PHE A 301 29.147 32.279 27.356 1.00 29.29 A ATOM 1826 CD1 PHE A 301 29.978 32.949 28.245 1.00 27.31 A ATOM 1827 CD2 PHE A 301 29.560 31.050 26.845 1.00 27.89 A ATOM 1828 CE1 PHE A 301 31.205 32.403 28.625 1.00 28.83 A ATOM 1829 CE2 PHE A 301 30.781 30.498 27.217 1.00 28.05 A ATOM 1830 CZ PHE A 301 31.605 31.175 28.110 1.00 28.27 A ATOM 1831 C PHE A 301 26.459 34.384 25.619 1.00 32.20 A ATOM 1832 O PHE A 301 25.946 35.261 26.317 1.00 32.36 A ATOM 1833 N PRO A 302 25.798 33.804 24.607 1.00 33.29 A ATOM 1834 CD PRO A 302 26.313 32.943 23.529 1.00 34.04 A ATOM 1835 CA PRO A 302 24.415 34.199 24.341 1.00 35.24 A ATOM 1836 CB PRO A 302 24.144 33.608 22.959 1.00 34.01 A ATOM 1837 CG PRO A 302 25.041 32.413 22.921 1.00 35.48 A ATOM 1838 C PRO A 302 23.567 33.561 25.444 1.00 37.39 A ATOM 1839 O PRO A 302 23.935 32.518 25.986 1.00 38.49 A ATOM 1840 N ALA A 303 22.447 34.188 25.783 1.00 39.36 A ATOM 1841 CA ALA A 303 21.572 33.692 26.843 1.00 40.65 A ATOM 1842 CB ALA A 303 20.280 34.506 26.862 1.00 41.66 A ATOM 1843 C ALA A 303 21.238 32.197 26.814 1.00 41.25 A ATOM 1844 O ALA A 303 21.253 31.537 27.854 1.00 43.16 A ATOM 1845 N ALA A 304 20.945 31.665 25.631 1.00 41.04 A ATOM 1846 CA ALA A 304 20.569 30.258 25.480 1.00 40.66 A ATOM 1847 CB ALA A 304 20.121 30.004 24.040 1.00 41.36 A ATOM 1848 C ALA A 304 21.628 29.223 25.876 1.00 39.61 A ATOM 1849 O ALA A 304 21.298 28.156 26.395 1.00 40.61 A ATOM 1850 N PHE A 305 22.891 29.543 25.617 1.00 36.21 A ATOM 1851 CA PHE A 305 24.022 28.662 25.909 1.00 32.08 A ATOM 1852 CB PHE A 305 25.259 29.519 26.187 1.00 29.46 A ATOM 1853 CG PHE A 305 26.536 28.917 25.690 1.00 28.15 A ATOM 1854 CD1 PHE A 305 27.146 27.875 26.377 1.00 26.20 A ATOM 1855 CD2 PHE A 305 27.127 29.386 24.521 1.00 27.05 A ATOM 1856 CE1 PHE A 305 28.330 27.308 25.908 1.00 26.92 A ATOM 1857 CE2 PHE A 305 28.312 28.826 24.042 1.00 26.62 A ATOM 1858 CZ PHE A 305 28.914 27.786 24.737 1.00 26.61 A ATOM 1859 C PHE A 305 23.811 27.664 27.057 1.00 30.09 A ATOM 1860 O PHE A 305 23.518 28.051 28.187 1.00 31.51 A ATOM 1861 N PHE A 306 23.964 26.378 26.758 1.00 27.01 A ATOM 1862 CA PHE A 306 23.801 25.334 27.769 1.00 26.30 A ATOM 1863 CB PHE A 306 24.157 23.970 27.170 1.00 25.03 A ATOM 1864 CG PHE A 306 23.548 23.725 25.815 1.00 27.24 A ATOM 1865 CD1 PHE A 306 22.170 23.831 25.622 1.00 28.40 A ATOM 1866 CD2 PHE A 306 24.350 23.386 24.728 1.00 27.84 A ATOM 1867 CE1 PHE A 306 21.601 23.603 24.365 1.00 28.05 A ATOM 1868 CE2 PHE A 306 23.792 23.155 23.465 1.00 28.31 A ATOM 1869 CZ PHE A 306 22.415 23.263 23.283 1.00 28.00 A ATOM 1870 C PHE A 306 24.711 25.652 28.961 1.00 26.23 A ATOM 1871 O PHE A 306 25.927 25.775 28.811 1.00 25.59 A ATOM 1872 N PRO A 307 24.125 25.796 30.163 1.00 26.67 A ATOM 1873 CD PRO A 307 22.685 25.625 30.430 1.00 27.95 A ATOM 1874 CA PRO A 307 24.842 26.110 31.405 1.00 26.59 A ATOM 1875 CB PRO A 307 23.795 25.832 32.481 1.00 26.14 A ATOM 1876 CG PRO A 307 22.531 26.250 31.803 1.00 27.86 A ATOM 1877 C PRO A 307 26.145 25.355 31.659 1.00 25.58 A ATOM 1878 O PRO A 307 27.189 25.964 31.900 1.00 22.65 A ATOM 1879 N LYS A 308 26.085 24.031 31.620 1.00 24.46 A ATOM 1880 CA LYS A 308 27.274 23.232 31.867 1.00 23.91 A ATOM 1881 CB LYS A 308 26.887 21.760 32.024 1.00 23.25 A ATOM 1882 CG LYS A 308 26.062 21.532 33.285 1.00 28.49 A ATOM 1883 CD LYS A 308 25.618 20.093 33.466 1.00 30.17 A ATOM 1884 CE LYS A 308 24.760 19.973 34.722 1.00 33.12 A ATOM 1885 NZ LYS A 308 24.122 18.636 34.860 1.00 34.13 A ATOM 1886 C LYS A 308 28.314 23.426 30.769 1.00 22.84 A ATOM 1887 O LYS A 308 29.514 23.411 31.042 1.00 22.46 A ATOM 1888 N ALA A 309 27.861 23.621 29.534 1.00 21.59 A ATOM 1889 CA ALA A 309 28.792 23.848 28.432 1.00 20.02 A ATOM 1890 CB ALA A 309 28.056 23.856 27.106 1.00 18.80 A ATOM 1891 C ALA A 309 29.481 25.191 28.662 1.00 21.41 A ATOM 1892 O ALA A 309 30.680 25.335 28.427 1.00 21.39 A ATOM 1893 N ARG A 310 28.717 26.179 29.121 1.00 21.39 A ATOM 1894 CA ARG A 310 29.290 27.494 29.388 1.00 22.02 A ATOM 1895 CB ARG A 310 28.213 28.479 29.854 1.00 22.39 A ATOM 1896 CG ARG A 310 28.806 29.756 30.436 1.00 25.30 A ATOM 1897 CD ARG A 310 27.780 30.852 30.664 1.00 28.33 A ATOM 1898 NE ARG A 310 28.420 32.039 31.230 1.00 30.18 A ATOM 1899 CZ ARG A 310 27.901 33.263 31.203 1.00 32.07 A ATOM 1900 NH1 ARG A 310 26.719 33.477 30.634 1.00 31.19 A ATOM 1901 NH2 ARG A 310 28.567 34.277 31.742 1.00 30.49 A ATOM 1902 C ARG A 310 30.376 27.388 30.458 1.00 21.65 A ATOM 1903 O ARG A 310 31.464 27.949 30.311 1.00 20.36 A ATOM 1904 N ASP A 311 30.074 26.677 31.541 1.00 19.57 A ATOM 1905 CA ASP A 311 31.043 26.512 32.615 1.00 20.18 A ATOM 1906 CB ASP A 311 30.460 25.649 33.739 1.00 20.39 A ATOM 1907 CG ASP A 311 31.439 25.446 34.881 1.00 23.35 A ATOM 1908 OD1 ASP A 311 32.158 24.428 34.885 1.00 24.91 A ATOM 1909 OD2 ASP A 311 31.500 26.312 35.776 1.00 26.96 A ATOM 1910 C ASP A 311 32.322 25.877 32.073 1.00 19.73 A ATOM 1911 O ASP A 311 33.422 26.289 32.439 1.00 19.30 A ATOM 1912 N LEU A 312 32.179 24.891 31.188 1.00 16.32 A ATOM 1913 CA LEU A 312 33.349 24.226 30.611 1.00 16.66 A ATOM 1914 CB LEU A 312 32.927 23.035 29.744 1.00 16.12 A ATOM 1915 CG LEU A 312 34.050 22.320 28.974 1.00 14.73 A ATOM 1916 CD1 LEU A 312 35.192 21.935 29.912 1.00 14.56 A ATOM 1917 CD2 LEU A 312 33.477 21.084 28.289 1.00 14.22 A ATOM 1918 C LEU A 312 34.181 25.189 29.774 1.00 16.61 A ATOM 1919 O LEU A 312 35.402 25.241 29.910 1.00 16.20 A ATOM 1920 N VAL A 313 33.515 25.949 28.908 1.00 16.20 A ATOM 1921 CA VAL A 313 34.207 26.907 28.058 1.00 15.37 A ATOM 1922 CB VAL A 313 33.216 27.648 27.130 1.00 16.42 A ATOM 1923 CG1 VAL A 313 33.915 28.796 26.426 1.00 16.93 A ATOM 1924 CG2 VAL A 313 32.644 26.672 26.103 1.00 17.88 A ATOM 1925 C VAL A 313 34.960 27.923 28.911 1.00 17.39 A ATOM 1926 O VAL A 313 36.093 28.294 28.591 1.00 18.00 A ATOM 1927 N GLU A 314 34.342 28.364 30.004 1.00 17.61 A ATOM 1928 CA GLU A 314 34.986 29.331 30.885 1.00 20.43 A ATOM 1929 CB GLU A 314 34.009 29.816 31.959 1.00 22.14 A ATOM 1930 CG GLU A 314 32.800 30.550 31.396 1.00 26.52 A ATOM 1931 CD GLU A 314 31.852 31.025 32.478 1.00 31.26 A ATOM 1932 OE1 GLU A 314 31.580 30.246 33.417 1.00 33.48 A ATOM 1933 OE2 GLU A 314 31.370 32.173 32.387 1.00 34.81 A ATOM 1934 C GLU A 314 36.217 28.721 31.539 1.00 19.15 A ATOM 1935 O GLU A 314 37.134 29.433 31.934 1.00 21.47 A ATOM 1936 N LYS A 315 36.245 27.400 31.651 1.00 19.51 A ATOM 1937 CA LYS A 315 37.394 26.749 32.258 1.00 19.17 A ATOM 1938 CB LYS A 315 36.946 25.514 33.043 1.00 18.84 A ATOM 1939 CG LYS A 315 36.280 25.885 34.368 1.00 19.62 A ATOM 1940 CD LYS A 315 35.653 24.696 35.073 1.00 19.22 A ATOM 1941 CE LYS A 315 35.070 25.095 36.427 1.00 21.00 A ATOM 1942 NZ LYS A 315 36.119 25.552 37.381 1.00 19.53 A ATOM 1943 C LYS A 315 38.452 26.393 31.218 1.00 18.96 A ATOM 1944 O LYS A 315 39.511 25.873 31.561 1.00 19.85 A ATOM 1945 N LEU A 316 38.164 26.691 29.950 1.00 17.08 A ATOM 1946 CA LEU A 316 39.102 26.429 28.854 1.00 16.41 A ATOM 1947 CB LEU A 316 38.414 25.636 27.738 1.00 13.81 A ATOM 1948 CG LEU A 316 38.028 24.201 28.115 1.00 14.39 A ATOM 1949 CD1 LEU A 316 37.139 23.597 27.031 1.00 12.38 A ATOM 1950 CD2 LEU A 316 39.302 23.373 28.309 1.00 12.77 A ATOM 1951 C LEU A 316 39.652 27.743 28.290 1.00 17.12 A ATOM 1952 O LEU A 316 40.851 27.860 28.023 1.00 16.53 A ATOM 1953 N LEU A 317 38.780 28.729 28.105 1.00 16.27 A ATOM 1954 CA LEU A 317 39.228 30.022 27.596 1.00 17.52 A ATOM 1955 CB LEU A 317 38.083 30.752 26.887 1.00 16.37 A ATOM 1956 CG LEU A 317 37.448 29.973 25.727 1.00 18.81 A ATOM 1957 CD1 LEU A 317 36.415 30.851 25.018 1.00 16.47 A ATOM 1958 CD2 LEU A 317 38.528 29.526 24.741 1.00 17.87 A ATOM 1959 C LEU A 317 39.745 30.841 28.774 1.00 18.27 A ATOM 1960 O LEU A 317 39.078 31.753 29.273 1.00 18.58 A ATOM 1961 N VAL A 318 40.937 30.475 29.229 1.00 18.02 A ATOM 1962 CA VAL A 318 41.593 31.141 30.342 1.00 18.85 A ATOM 1963 CB VAL A 318 41.846 30.153 31.500 1.00 19.91 A ATOM 1964 CG1 VAL A 318 42.590 30.848 32.634 1.00 20.01 A ATOM 1965 CG2 VAL A 318 40.520 29.584 31.990 1.00 19.44 A ATOM 1966 C VAL A 318 42.923 31.657 29.811 1.00 19.67 A ATOM 1967 O VAL A 318 43.690 30.902 29.208 1.00 18.26 A ATOM 1968 N LEU A 319 43.197 32.939 30.028 1.00 20.07 A ATOM 1969 CA LEU A 319 44.436 33.533 29.538 1.00 20.98 A ATOM 1970 CB LEU A 319 44.521 35.002 29.968 1.00 21.64 A ATOM 1971 CG LEU A 319 43.418 35.908 29.408 1.00 24.38 A ATOM 1972 CD1 LEU A 319 43.606 37.332 29.935 1.00 23.28 A ATOM 1973 CD2 LEU A 319 43.453 35.887 27.875 1.00 24.33 A ATOM 1974 C LEU A 319 45.680 32.774 29.994 1.00 20.38 A ATOM 1975 O LEU A 319 46.568 32.496 29.192 1.00 21.34 A ATOM 1976 N ASP A 320 45.742 32.440 31.280 1.00 20.22 A ATOM 1977 CA ASP A 320 46.879 31.707 31.833 1.00 20.90 A ATOM 1978 CB ASP A 320 46.842 31.760 33.365 1.00 20.76 A ATOM 1979 CG ASP A 320 48.049 31.102 34.004 1.00 21.51 A ATOM 1980 OD1 ASP A 320 48.669 30.226 33.367 1.00 23.46 A ATOM 1981 OD2 ASP A 320 48.371 31.450 35.159 1.00 23.89 A ATOM 1982 C ASP A 320 46.814 30.247 31.367 1.00 20.06 A ATOM 1983 O ASP A 320 45.988 29.476 31.840 1.00 20.54 A ATOM 1984 N ALA A 321 47.700 29.876 30.451 1.00 20.68 A ATOM 1985 CA ALA A 321 47.733 28.522 29.903 1.00 22.04 A ATOM 1986 CB ALA A 321 48.860 28.411 28.881 1.00 20.75 A ATOM 1987 C ALA A 321 47.858 27.400 30.940 1.00 21.62 A ATOM 1988 O ALA A 321 47.482 26.259 30.665 1.00 21.99 A ATOM 1989 N THR A 322 48.372 27.715 32.127 1.00 20.89 A ATOM 1990 CA THR A 322 48.531 26.698 33.167 1.00 20.82 A ATOM 1991 CB THR A 322 49.670 27.051 34.146 1.00 19.47 A ATOM 1992 OG1 THR A 322 49.341 28.253 34.848 1.00 20.19 A ATOM 1993 CG2 THR A 322 50.981 27.249 33.394 1.00 21.59 A ATOM 1994 C THR A 322 47.264 26.498 33.983 1.00 19.55 A ATOM 1995 O THR A 322 47.235 25.673 34.894 1.00 21.13 A ATOM 1996 N LYS A 323 46.216 27.248 33.661 1.00 19.33 A ATOM 1997 CA LYS A 323 44.962 27.122 34.392 1.00 21.20 A ATOM 1998 CB LYS A 323 44.580 28.460 35.030 1.00 23.75 A ATOM 1999 CG LYS A 323 45.562 28.933 36.084 1.00 28.45 A ATOM 2000 CD LYS A 323 45.055 30.177 36.799 1.00 33.76 A ATOM 2001 CE LYS A 323 46.087 30.678 37.802 1.00 36.15 A ATOM 2002 NZ LYS A 323 46.532 29.569 38.693 1.00 37.34 A ATOM 2003 C LYS A 323 43.806 26.614 33.539 1.00 20.68 A ATOM 2004 O LYS A 323 42.649 26.757 33.915 1.00 20.42 A ATOM 2005 N ARG A 324 44.114 26.019 32.392 1.00 19.97 A ATOM 2006 CA ARG A 324 43.060 25.494 31.531 1.00 17.98 A ATOM 2007 CB ARG A 324 43.461 25.609 30.061 1.00 15.95 A ATOM 2008 CG ARG A 324 43.534 27.050 29.603 1.00 17.34 A ATOM 2009 CD ARG A 324 43.996 27.194 28.172 1.00 19.80 A ATOM 2010 NE ARG A 324 44.438 28.565 27.944 1.00 16.93 A ATOM 2011 CZ ARG A 324 45.410 28.908 27.108 1.00 19.88 A ATOM 2012 NH1 ARG A 324 46.045 27.978 26.398 1.00 14.58 A ATOM 2013 NH2 ARG A 324 45.774 30.181 27.015 1.00 16.51 A ATOM 2014 C ARG A 324 42.762 24.046 31.883 1.00 18.32 A ATOM 2015 O ARG A 324 43.673 23.222 32.006 1.00 18.20 A ATOM 2016 N LEU A 325 41.479 23.748 32.055 1.00 18.32 A ATOM 2017 CA LEU A 325 41.050 22.403 32.395 1.00 17.79 A ATOM 2018 CB LEU A 325 39.523 22.335 32.425 1.00 17.03 A ATOM 2019 CG LEU A 325 38.896 21.125 33.116 1.00 15.91 A ATOM 2020 CD1 LEU A 325 39.392 21.048 34.557 1.00 15.93 A ATOM 2021 CD2 LEU A 325 37.375 21.255 33.084 1.00 16.56 A ATOM 2022 C LEU A 325 41.599 21.433 31.356 1.00 18.68 A ATOM 2023 O LEU A 325 41.347 21.586 30.157 1.00 18.28 A ATOM 2024 N GLY A 326 42.354 20.439 31.821 1.00 18.18 A ATOM 2025 CA GLY A 326 42.931 19.462 30.915 1.00 16.36 A ATOM 2026 C GLY A 326 44.443 19.558 30.807 1.00 19.15 A ATOM 2027 O GLY A 326 45.093 18.592 30.404 1.00 19.52 A ATOM 2028 N CYS A 327 45.016 20.708 31.161 1.00 18.16 A ATOM 2029 CA CYS A 327 46.463 20.867 31.075 1.00 19.30 A ATOM 2030 CB CYS A 327 46.856 22.350 31.058 1.00 20.22 A ATOM 2031 SG CYS A 327 46.782 23.200 32.649 1.00 21.97 A ATOM 2032 C CYS A 327 47.169 20.157 32.228 1.00 20.22 A ATOM 2033 O CYS A 327 46.561 19.828 33.246 1.00 17.92 A ATOM 2034 N GLU A 328 48.463 19.933 32.053 1.00 20.51 A ATOM 2035 CA GLU A 328 49.274 19.244 33.042 1.00 23.34 A ATOM 2036 CB GLU A 328 50.710 19.139 32.507 1.00 28.68 A ATOM 2037 CG GLU A 328 50.754 18.367 31.175 1.00 38.24 A ATOM 2038 CD GLU A 328 52.067 18.500 30.414 1.00 43.23 A ATOM 2039 OE1 GLU A 328 52.535 19.643 30.218 1.00 46.22 A ATOM 2040 OE2 GLU A 328 52.618 17.459 29.991 1.00 44.90 A ATOM 2041 C GLU A 328 49.234 19.876 34.435 1.00 22.11 A ATOM 2042 O GLU A 328 49.147 19.161 35.437 1.00 20.27 A ATOM 2043 N GLU A 329 49.276 21.204 34.506 1.00 18.40 A ATOM 2044 CA GLU A 329 49.248 21.875 35.801 1.00 20.13 A ATOM 2045 CB GLU A 329 49.587 23.363 35.657 1.00 20.36 A ATOM 2046 CG GLU A 329 51.014 23.651 35.190 1.00 24.05 A ATOM 2047 CD GLU A 329 51.191 23.518 33.688 1.00 25.93 A ATOM 2048 OE1 GLU A 329 50.213 23.154 32.995 1.00 26.61 A ATOM 2049 OE2 GLU A 329 52.311 23.781 33.198 1.00 27.19 A ATOM 2050 C GLU A 329 47.890 21.718 36.480 1.00 19.36 A ATOM 2051 O GLU A 329 47.775 21.879 37.694 1.00 18.74 A ATOM 2052 N MET A 330 46.863 21.415 35.691 1.00 17.28 A ATOM 2053 CA MET A 330 45.520 21.220 36.229 1.00 16.38 A ATOM 2054 CB MET A 330 44.474 21.833 35.294 1.00 17.65 A ATOM 2055 CG MET A 330 44.460 23.365 35.311 1.00 22.95 A ATOM 2056 SD MET A 330 44.186 24.026 36.979 1.00 26.78 A ATOM 2057 CE MET A 330 42.435 23.712 37.186 1.00 24.69 A ATOM 2058 C MET A 330 45.257 19.730 36.422 1.00 14.30 A ATOM 2059 O MET A 330 44.127 19.304 36.629 1.00 15.39 A ATOM 2060 N GLU A 331 46.327 18.949 36.346 1.00 15.60 A ATOM 2061 CA GLU A 331 46.289 17.501 36.531 1.00 17.08 A ATOM 2062 CB GLU A 331 45.607 17.155 37.862 1.00 17.00 A ATOM 2063 CG GLU A 331 46.070 18.027 39.038 1.00 17.46 A ATOM 2064 CD GLU A 331 47.591 18.179 39.145 1.00 20.16 A ATOM 2065 OE1 GLU A 331 48.034 19.073 39.896 1.00 21.39 A ATOM 2066 OE2 GLU A 331 48.345 17.420 38.500 1.00 18.87 A ATOM 2067 C GLU A 331 45.697 16.658 35.398 1.00 17.80 A ATOM 2068 O GLU A 331 45.107 15.602 35.636 1.00 20.40 A ATOM 2069 N GLY A 332 45.844 17.133 34.167 1.00 16.23 A ATOM 2070 CA GLY A 332 45.420 16.353 33.015 1.00 14.10 A ATOM 2071 C GLY A 332 43.982 16.154 32.596 1.00 13.54 A ATOM 2072 O GLY A 332 43.063 16.864 33.017 1.00 11.96 A ATOM 2073 N TYR A 333 43.804 15.141 31.750 1.00 14.37 A ATOM 2074 CA TYR A 333 42.510 14.806 31.182 1.00 13.56 A ATOM 2075 CB TYR A 333 42.722 13.892 29.968 1.00 15.00 A ATOM 2076 CG TYR A 333 43.153 14.683 28.752 1.00 16.46 A ATOM 2077 CD1 TYR A 333 42.206 15.172 27.849 1.00 15.29 A ATOM 2078 CE1 TYR A 333 42.573 16.002 26.794 1.00 13.42 A ATOM 2079 CD2 TYR A 333 44.490 15.039 28.561 1.00 14.91 A ATOM 2080 CE2 TYR A 333 44.872 15.877 27.499 1.00 14.87 A ATOM 2081 CZ TYR A 333 43.902 16.353 26.626 1.00 15.61 A ATOM 2082 OH TYR A 333 44.244 17.197 25.599 1.00 17.29 A ATOM 2083 C TYR A 333 41.470 14.230 32.127 1.00 15.23 A ATOM 2084 O TYR A 333 40.278 14.323 31.846 1.00 16.63 A ATOM 2085 N GLY A 334 41.907 13.650 33.244 1.00 15.50 A ATOM 2086 CA GLY A 334 40.957 13.100 34.202 1.00 15.07 A ATOM 2087 C GLY A 334 39.925 14.146 34.616 1.00 16.40 A ATOM 2088 O GLY A 334 38.724 13.946 34.433 1.00 15.05 A ATOM 2089 N PRO A 335 40.366 15.278 35.184 1.00 14.96 A ATOM 2090 CD PRO A 335 41.727 15.531 35.689 1.00 15.88 A ATOM 2091 CA PRO A 335 39.444 16.339 35.606 1.00 15.29 A ATOM 2092 CB PRO A 335 40.383 17.397 36.178 1.00 13.19 A ATOM 2093 CG PRO A 335 41.485 16.569 36.758 1.00 13.81 A ATOM 2094 C PRO A 335 38.594 16.877 34.448 1.00 15.84 A ATOM 2095 O PRO A 335 37.423 17.204 34.631 1.00 14.84 A ATOM 2096 N LEU A 336 39.184 16.971 33.257 1.00 16.12 A ATOM 2097 CA LEU A 336 38.450 17.465 32.094 1.00 15.52 A ATOM 2098 CB LEU A 336 39.396 17.653 30.898 1.00 14.39 A ATOM 2099 CG LEU A 336 38.770 17.991 29.538 1.00 15.46 A ATOM 2100 CD1 LEU A 336 37.836 19.182 29.662 1.00 11.25 A ATOM 2101 CD2 LEU A 336 39.884 18.285 28.528 1.00 14.11 A ATOM 2102 C LEU A 336 37.321 16.508 31.714 1.00 16.28 A ATOM 2103 O LEU A 336 36.176 16.921 31.540 1.00 15.51 A ATOM 2104 N LYS A 337 37.640 15.225 31.592 1.00 17.22 A ATOM 2105 CA LYS A 337 36.624 14.243 31.235 1.00 17.39 A ATOM 2106 CB LYS A 337 37.293 12.900 30.921 1.00 17.68 A ATOM 2107 CG LYS A 337 38.170 12.994 29.676 1.00 22.31 A ATOM 2108 CD LYS A 337 39.213 11.892 29.592 1.00 24.60 A ATOM 2109 CE LYS A 337 38.620 10.560 29.189 1.00 24.76 A ATOM 2110 NZ LYS A 337 39.710 9.560 28.997 1.00 25.05 A ATOM 2111 C LYS A 337 35.577 14.096 32.342 1.00 17.33 A ATOM 2112 O LYS A 337 34.456 13.652 32.090 1.00 14.42 A ATOM 2113 N ALA A 338 35.928 14.500 33.559 1.00 15.83 A ATOM 2114 CA ALA A 338 34.989 14.395 34.674 1.00 17.52 A ATOM 2115 CB ALA A 338 35.749 14.167 35.980 1.00 19.68 A ATOM 2116 C ALA A 338 34.095 15.621 34.804 1.00 18.83 A ATOM 2117 O ALA A 338 33.252 15.687 35.695 1.00 18.94 A ATOM 2118 N HIS A 339 34.262 16.596 33.918 1.00 19.42 A ATOM 2119 CA HIS A 339 33.438 17.796 34.004 1.00 19.28 A ATOM 2120 CB HIS A 339 33.865 18.819 32.949 1.00 19.20 A ATOM 2121 CG HIS A 339 33.163 20.134 33.074 1.00 20.26 A ATOM 2122 CD2 HIS A 339 33.549 21.299 33.649 1.00 18.95 A ATOM 2123 ND1 HIS A 339 31.880 20.340 32.612 1.00 19.10 A ATOM 2124 CE1 HIS A 339 31.506 21.576 32.896 1.00 22.19 A ATOM 2125 NE2 HIS A 339 32.500 22.179 33.525 1.00 21.98 A ATOM 2126 C HIS A 339 31.957 17.448 33.845 1.00 19.13 A ATOM 2127 O HIS A 339 31.597 16.576 33.061 1.00 19.52 A ATOM 2128 N PRO A 340 31.079 18.125 34.606 1.00 19.80 A ATOM 2129 CD PRO A 340 31.424 19.119 35.640 1.00 19.08 A ATOM 2130 CA PRO A 340 29.630 17.900 34.569 1.00 20.52 A ATOM 2131 CB PRO A 340 29.091 19.058 35.396 1.00 20.74 A ATOM 2132 CG PRO A 340 30.146 19.207 36.454 1.00 19.20 A ATOM 2133 C PRO A 340 29.000 17.834 33.176 1.00 21.42 A ATOM 2134 O PRO A 340 28.049 17.088 32.955 1.00 22.48 A ATOM 2135 N PHE A 341 29.528 18.606 32.237 1.00 21.33 A ATOM 2136 CA PHE A 341 28.985 18.610 30.886 1.00 21.57 A ATOM 2137 CB PHE A 341 29.739 19.624 30.017 1.00 21.64 A ATOM 2138 CG PHE A 341 29.207 19.740 28.613 1.00 23.18 A ATOM 2139 CD1 PHE A 341 27.903 20.171 28.382 1.00 22.58 A ATOM 2140 CD2 PHE A 341 30.013 19.431 27.522 1.00 21.95 A ATOM 2141 CE1 PHE A 341 27.410 20.292 27.082 1.00 23.54 A ATOM 2142 CE2 PHE A 341 29.533 19.548 26.220 1.00 21.83 A ATOM 2143 CZ PHE A 341 28.228 19.980 25.998 1.00 23.23 A ATOM 2144 C PHE A 341 29.055 17.226 30.237 1.00 21.84 A ATOM 2145 O PHE A 341 28.232 16.896 29.389 1.00 20.37 A ATOM 2146 N PHE A 342 30.034 16.422 30.640 1.00 20.51 A ATOM 2147 CA PHE A 342 30.221 15.085 30.077 1.00 23.01 A ATOM 2148 CB PHE A 342 31.710 14.809 29.850 1.00 18.00 A ATOM 2149 CG PHE A 342 32.398 15.812 28.971 1.00 17.05 A ATOM 2150 CD1 PHE A 342 32.010 15.987 27.652 1.00 17.78 A ATOM 2151 CD2 PHE A 342 33.487 16.534 29.450 1.00 15.72 A ATOM 2152 CE1 PHE A 342 32.702 16.867 26.811 1.00 18.08 A ATOM 2153 CE2 PHE A 342 34.184 17.414 28.617 1.00 17.45 A ATOM 2154 CZ PHE A 342 33.790 17.578 27.298 1.00 16.56 A ATOM 2155 C PHE A 342 29.679 13.972 30.976 1.00 24.95 A ATOM 2156 O PHE A 342 30.002 12.798 30.777 1.00 23.95 A ATOM 2157 N GLU A 343 28.861 14.333 31.958 1.00 27.35 A ATOM 2158 CA GLU A 343 28.325 13.349 32.897 1.00 30.28 A ATOM 2159 CB GLU A 343 27.187 13.964 33.716 1.00 32.20 A ATOM 2160 CG GLU A 343 26.581 12.991 34.714 1.00 39.71 A ATOM 2161 CD GLU A 343 25.628 13.661 35.688 1.00 44.72 A ATOM 2162 OE1 GLU A 343 24.661 14.314 35.234 1.00 47.55 A ATOM 2163 OE2 GLU A 343 25.847 13.526 36.911 1.00 46.89 A ATOM 2164 C GLU A 343 27.852 12.017 32.305 1.00 28.98 A ATOM 2165 O GLU A 343 28.225 10.952 32.800 1.00 31.73 A ATOM 2166 N SER A 344 27.037 12.067 31.258 1.00 26.09 A ATOM 2167 CA SER A 344 26.520 10.838 30.656 1.00 28.36 A ATOM 2168 CB SER A 344 25.129 11.089 30.067 1.00 28.73 A ATOM 2169 OG SER A 344 25.203 11.942 28.940 1.00 30.91 A ATOM 2170 C SER A 344 27.407 10.214 29.577 1.00 27.66 A ATOM 2171 O SER A 344 26.987 9.281 28.900 1.00 28.66 A ATOM 2172 N VAL A 345 28.627 10.715 29.419 1.00 26.75 A ATOM 2173 CA VAL A 345 29.534 10.183 28.402 1.00 23.44 A ATOM 2174 CB VAL A 345 30.565 11.256 27.950 1.00 23.10 A ATOM 2175 CG1 VAL A 345 31.589 10.631 26.995 1.00 22.24 A ATOM 2176 CG2 VAL A 345 29.854 12.418 27.275 1.00 20.05 A ATOM 2177 C VAL A 345 30.326 8.957 28.855 1.00 24.26 A ATOM 2178 O VAL A 345 30.876 8.930 29.960 1.00 22.83 A ATOM 2179 N THR A 346 30.374 7.942 27.997 1.00 21.77 A ATOM 2180 CA THR A 346 31.153 6.740 28.272 1.00 23.70 A ATOM 2181 CB THR A 346 30.391 5.455 27.857 1.00 26.53 A ATOM 2182 OG1 THR A 346 29.248 5.284 28.706 1.00 29.98 A ATOM 2183 CG2 THR A 346 31.289 4.231 27.990 1.00 24.28 A ATOM 2184 C THR A 346 32.383 6.945 27.385 1.00 23.43 A ATOM 2185 O THR A 346 32.306 6.827 26.160 1.00 24.50 A ATOM 2186 N TRP A 347 33.508 7.270 28.013 1.00 22.98 A ATOM 2187 CA TRP A 347 34.744 7.569 27.300 1.00 23.81 A ATOM 2188 CB TRP A 347 35.683 8.352 28.219 1.00 22.54 A ATOM 2189 CG TRP A 347 35.128 9.658 28.693 1.00 20.61 A ATOM 2190 CD2 TRP A 347 35.257 10.927 28.040 1.00 19.11 A ATOM 2191 CE2 TRP A 347 34.581 11.881 28.838 1.00 18.39 A ATOM 2192 CE3 TRP A 347 35.878 11.351 26.858 1.00 18.16 A ATOM 2193 CD1 TRP A 347 34.397 9.883 29.828 1.00 18.35 A ATOM 2194 NE1 TRP A 347 34.065 11.218 29.923 1.00 19.51 A ATOM 2195 CZ2 TRP A 347 34.510 13.234 28.491 1.00 16.88 A ATOM 2196 CZ3 TRP A 347 35.808 12.701 26.511 1.00 17.23 A ATOM 2197 CH2 TRP A 347 35.127 13.624 27.327 1.00 18.16 A ATOM 2198 C TRP A 347 35.538 6.429 26.675 1.00 25.79 A ATOM 2199 O TRP A 347 36.304 6.654 25.742 1.00 24.67 A ATOM 2200 N ALA A 348 35.360 5.215 27.183 1.00 27.10 A ATOM 2201 CA ALA A 348 36.116 4.063 26.697 1.00 27.46 A ATOM 2202 CB ALA A 348 35.899 2.869 27.636 1.00 27.09 A ATOM 2203 C ALA A 348 35.895 3.620 25.256 1.00 27.18 A ATOM 2204 O ALA A 348 36.830 3.148 24.613 1.00 29.41 A ATOM 2205 N ASN A 349 34.682 3.769 24.735 1.00 26.55 A ATOM 2206 CA ASN A 349 34.418 3.310 23.375 1.00 27.28 A ATOM 2207 CB ASN A 349 33.700 1.962 23.444 1.00 29.37 A ATOM 2208 CG ASN A 349 32.299 2.088 24.013 1.00 30.92 A ATOM 2209 OD1 ASN A 349 32.045 2.942 24.859 1.00 30.17 A ATOM 2210 ND2 ASN A 349 31.386 1.237 23.553 1.00 33.52 A ATOM 2211 C ASN A 349 33.599 4.265 22.509 1.00 26.47 A ATOM 2212 O ASN A 349 32.669 3.843 21.819 1.00 25.87 A ATOM 2213 N LEU A 350 33.947 5.543 22.518 1.00 24.45 A ATOM 2214 CA LEU A 350 33.203 6.510 21.721 1.00 23.14 A ATOM 2215 CB LEU A 350 33.837 7.898 21.848 1.00 23.22 A ATOM 2216 CG LEU A 350 33.659 8.605 23.191 1.00 21.05 A ATOM 2217 CD1 LEU A 350 34.646 9.756 23.293 1.00 19.36 A ATOM 2218 CD2 LEU A 350 32.220 9.094 23.319 1.00 18.78 A ATOM 2219 C LEU A 350 33.082 6.152 20.240 1.00 22.60 A ATOM 2220 O LEU A 350 32.011 6.296 19.650 1.00 21.15 A ATOM 2221 N HIS A 351 34.165 5.689 19.627 1.00 23.13 A ATOM 2222 CA HIS A 351 34.089 5.387 18.204 1.00 27.83 A ATOM 2223 CB HIS A 351 35.506 5.325 17.596 1.00 29.36 A ATOM 2224 CG HIS A 351 36.082 3.950 17.493 1.00 32.07 A ATOM 2225 CD2 HIS A 351 36.611 3.128 18.431 1.00 32.39 A ATOM 2226 ND1 HIS A 351 36.197 3.285 16.291 1.00 33.02 A ATOM 2227 CE1 HIS A 351 36.775 2.113 16.493 1.00 33.58 A ATOM 2228 NE2 HIS A 351 37.036 1.992 17.782 1.00 31.76 A ATOM 2229 C HIS A 351 33.258 4.144 17.874 1.00 28.12 A ATOM 2230 O HIS A 351 33.015 3.847 16.707 1.00 29.49 A ATOM 2231 N GLN A 352 32.800 3.442 18.908 1.00 29.28 A ATOM 2232 CA GLN A 352 31.963 2.255 18.726 1.00 29.67 A ATOM 2233 CB GLN A 352 32.366 1.145 19.694 1.00 30.56 A ATOM 2234 CG GLN A 352 33.169 0.041 19.041 1.00 30.88 A ATOM 2235 CD GLN A 352 34.493 −0.186 19.729 1.00 31.21 A ATOM 2236 OE1 GLN A 352 34.541 −0.450 20.928 1.00 30.76 A ATOM 2237 NE2 GLN A 352 35.578 −0.084 18.971 1.00 32.30 A ATOM 2238 C GLN A 352 30.504 2.638 18.963 1.00 30.42 A ATOM 2239 O GLN A 352 29.595 1.831 18.770 1.00 29.01 A ATOM 2240 N GLN A 353 30.290 3.875 19.397 1.00 27.64 A ATOM 2241 CA GLN A 353 28.948 4.365 19.652 1.00 27.42 A ATOM 2242 CB GLN A 353 28.977 5.401 20.775 1.00 25.77 A ATOM 2243 CG GLN A 353 29.408 4.837 22.115 1.00 27.34 A ATOM 2244 CD GLN A 353 29.638 5.914 23.156 1.00 27.19 A ATOM 2245 OE1 GLN A 353 28.875 6.872 23.252 1.00 28.29 A ATOM 2246 NE2 GLN A 353 30.687 5.753 23.951 1.00 28.79 A ATOM 2247 C GLN A 353 28.375 4.989 18.385 1.00 29.00 A ATOM 2248 O GLN A 353 29.118 5.455 17.516 1.00 29.14 A ATOM 2249 N THR A 354 27.053 4.984 18.276 1.00 27.31 A ATOM 2250 CA THR A 354 26.390 5.568 17.119 1.00 27.85 A ATOM 2251 CB THR A 354 24.991 4.941 16.904 1.00 30.69 A ATOM 2252 OG1 THR A 354 25.132 3.532 16.665 1.00 30.07 A ATOM 2253 CG2 THR A 354 24.289 5.585 15.709 1.00 29.58 A ATOM 2254 C THR A 354 26.244 7.062 17.376 1.00 26.85 A ATOM 2255 O THR A 354 25.592 7.475 18.329 1.00 25.77 A ATOM 2256 N PRO A 355 26.867 7.898 16.533 1.00 27.22 A ATOM 2257 CD PRO A 355 27.792 7.588 15.431 1.00 25.89 A ATOM 2258 CA PRO A 355 26.763 9.346 16.734 1.00 27.23 A ATOM 2259 CB PRO A 355 27.625 9.915 15.609 1.00 24.91 A ATOM 2260 CG PRO A 355 28.643 8.838 15.385 1.00 25.54 A ATOM 2261 C PRO A 355 25.322 9.837 16.641 1.00 28.07 A ATOM 2262 O PRO A 355 24.548 9.364 15.810 1.00 27.24 A ATOM 2263 N PRO A 356 24.941 10.792 17.500 1.00 28.28 A ATOM 2264 CD PRO A 356 25.752 11.560 18.462 1.00 28.31 A ATOM 2265 CA PRO A 356 23.572 11.306 17.448 1.00 28.44 A ATOM 2266 CB PRO A 356 23.539 12.301 18.604 1.00 28.11 A ATOM 2267 CG PRO A 356 24.946 12.832 18.612 1.00 26.86 A ATOM 2268 C PRO A 356 23.363 11.978 16.097 1.00 29.25 A ATOM 2269 O PRO A 356 24.304 12.537 15.529 1.00 27.27 A ATOM 2270 N ALA A 357 22.143 11.910 15.575 1.00 30.45 A ATOM 2271 CA ALA A 357 21.848 12.521 14.287 1.00 32.81 A ATOM 2272 CB ALA A 357 20.507 12.019 13.757 1.00 31.99 A ATOM 2273 C ALA A 357 21.824 14.035 14.448 1.00 35.05 A ATOM 2274 O ALA A 357 21.194 14.561 15.369 1.00 35.04 A ATOM 2275 N LEU A 358 22.516 14.730 13.552 1.00 37.81 A ATOM 2276 CA LEU A 358 22.578 16.185 13.597 1.00 42.15 A ATOM 2277 CB LEU A 358 23.679 16.681 12.658 1.00 39.54 A ATOM 2278 CG LEU A 358 25.086 16.285 13.109 1.00 39.51 A ATOM 2279 CD1 LEU A 358 26.102 16.686 12.062 1.00 39.29 A ATOM 2280 CD2 LEU A 358 25.395 16.953 14.445 1.00 40.01 A ATOM 2281 C LEU A 358 21.241 16.837 13.242 1.00 45.91 A ATOM 2282 O LEU A 358 20.874 16.927 12.069 1.00 45.71 A ATOM 2283 N THR A 359 20.530 17.290 14.275 1.00 50.06 A ATOM 2284 CA THR A 359 19.223 17.939 14.140 1.00 53.73 A ATOM 2285 CB THR A 359 19.353 19.428 13.726 1.00 54.04 A ATOM 2286 OG1 THR A 359 19.995 19.521 12.448 1.00 56.35 A ATOM 2287 CG2 THR A 359 20.158 20.204 14.763 1.00 54.32 A ATOM 2288 C THR A 359 18.309 17.236 13.139 1.00 54.47 A ATOM 2289 O THR A 359 18.483 16.016 12.930 1.00 55.90 A ATOM 2290 OXT THR A 359 17.407 17.908 12.595 1.00 56.97 A ATOM 2291 OH2 TIP S 1 42.566 19.118 34.302 1.00 15.09 S ATOM 2292 OH2 TIP S 2 41.052 32.378 19.857 1.00 15.82 S ATOM 2293 OH2 TIP S 3 37.014 33.030 17.747 1.00 16.95 S ATOM 2294 OH2 TIP S 5 45.353 24.370 18.152 1.00 16.85 S ATOM 2295 OH2 TIP S 6 31.896 13.930 33.235 1.00 20.42 S ATOM 2296 OH2 TIP S 7 50.351 22.781 28.249 1.00 21.14 S ATOM 2297 OH2 TIP S 8 45.246 −0.589 −0.734 1.00 17.74 S ATOM 2298 OH2 TIP S 11 46.249 −0.348 −8.523 1.00 21.32 S ATOM 2299 OH2 TIP S 14 45.756 11.148 29.680 1.00 21.94 S ATOM 2300 OH2 TIP S 15 44.273 13.157 34.592 1.00 15.61 S ATOM 2301 OH2 TIP S 17 53.598 3.722 −1.720 1.00 21.45 S ATOM 2302 OH2 TIP S 18 46.049 13.087 31.565 1.00 20.35 S ATOM 2303 OH2 TIP S 19 53.422 22.401 −3.280 1.00 23.26 S ATOM 2304 OH2 TIP S 20 34.587 7.922 5.383 1.00 22.58 S ATOM 2305 OH2 TIP S 21 45.053 27.379 19.376 1.00 29.60 S ATOM 2306 OH2 TIP S 23 28.899 36.416 28.633 1.00 31.68 S ATOM 2307 OH2 TIP S 24 35.531 11.645 −8.219 1.00 23.45 S ATOM 2308 OH2 TIP S 25 47.364 28.787 19.612 1.00 23.03 S ATOM 2309 OH2 TIP S 27 48.859 21.588 12.634 1.00 23.76 S ATOM 2310 OH2 TIP S 29 48.805 8.920 23.626 1.00 22.23 S ATOM 2311 OH2 TIP S 31 48.619 7.247 10.112 1.00 21.32 S ATOM 2312 OH2 TIP S 34 44.824 28.720 15.621 1.00 25.27 S ATOM 2313 OH2 TIP S 35 26.030 12.634 13.407 1.00 21.61 S ATOM 2314 OH2 TIP S 36 50.462 19.810 40.066 1.00 25.45 S ATOM 2315 OH2 TIP S 37 39.631 23.510 −0.239 1.00 30.88 S ATOM 2316 OH2 TIP S 40 44.734 42.655 10.346 1.00 30.84 S ATOM 2317 OH2 TIP S 41 54.653 3.902 1.503 1.00 27.14 S ATOM 2318 OH2 TIP S 45 45.693 21.923 39.754 1.00 28.30 S ATOM 2319 OH2 TIP S 47 47.820 16.413 7.805 1.00 25.73 S ATOM 2320 OH2 TIP S 48 50.292 31.412 29.642 1.00 32.79 S ATOM 2321 OH2 TIP S 49 26.056 16.646 34.827 1.00 29.80 S ATOM 2322 OH2 TIP S 52 31.714 10.996 31.855 1.00 29.15 S ATOM 2323 OH2 TIP S 53 46.108 23.843 −4.299 1.00 24.21 S ATOM 2324 OH2 TIP S 54 37.645 11.206 34.448 1.00 28.56 S ATOM 2325 OH2 TIP S 55 26.371 28.513 12.142 1.00 32.08 S ATOM 2326 OH2 TIP S 58 33.564 19.700 3.483 1.00 28.28 S ATOM 2327 OH2 TIP S 64 48.295 −0.632 14.280 1.00 32.13 S ATOM 2328 OH2 TIP S 65 40.064 26.036 34.324 1.00 24.17 S ATOM 2329 OH2 TIP S 66 29.570 3.958 14.729 1.00 28.94 S ATOM 2330 OH2 TIP S 72 60.085 11.604 6.814 1.00 38.35 S ATOM 2331 OH2 TIP S 73 39.203 44.403 18.686 1.00 26.61 S ATOM 2332 OH2 TIP S 76 47.312 12.366 27.366 1.00 28.51 S ATOM 2333 OH2 TIP S 80 43.862 33.771 33.329 1.00 28.82 S ATOM 2334 OH2 TIP S 81 57.890 13.106 2.128 1.00 40.62 S ATOM 2335 OH2 TIP S 82 41.663 34.381 32.043 1.00 19.35 S ATOM 2336 OH2 TIP S 85 50.974 40.331 19.200 1.00 21.14 S ATOM 2337 OH2 TIP S 88 47.925 −0.832 −6.556 1.00 24.11 S ATOM 2338 OH2 TIP S 90 27.231 28.336 33.481 1.00 27.64 S ATOM 2339 OH2 TIP S 91 43.651 −7.101 −7.995 1.00 24.33 S ATOM 2340 OH2 TIP S 92 49.325 4.387 19.370 1.00 28.02 S ATOM 2341 OH2 TIP S 93 46.231 11.549 33.898 1.00 29.40 S ATOM 2342 OH2 TIP S 94 63.889 24.831 1.168 1.00 26.53 S ATOM 2343 OH2 TIP S 96 56.396 4.952 −6.749 1.00 28.00 S ATOM 2344 OH2 TIP S 98 35.510 27.986 11.558 1.00 29.24 S ATOM 2345 OH2 TIP S 100 49.942 24.366 30.265 1.00 31.61 S ATOM 2346 OH2 TIP S 101 56.121 7.113 −8.298 1.00 31.57 S ATOM 2347 OH2 TIP S 102 58.318 19.957 −8.378 1.00 26.95 S ATOM 2348 OH2 TIP S 103 49.647 22.446 39.624 1.00 40.57 S ATOM 2349 OH2 TIP S 104 45.359 7.052 13.052 1.00 26.27 S ATOM 2350 OH2 TIP S 105 37.150 32.340 32.346 1.00 34.45 S ATOM 2351 OH2 TIP S 107 43.465 40.457 8.240 1.00 40.48 S ATOM 2352 OH2 TIP S 119 36.644 8.257 13.418 1.00 30.70 S ATOM 2353 OH2 TIP S 123 41.912 −8.974 −8.264 1.00 26.08 S ATOM 2354 OH2 TIP S 124 62.424 15.800 −7.411 1.00 24.08 S ATOM 2355 OH2 TIP S 126 37.266 18.656 −9.097 1.00 28.99 S ATOM 2356 OH2 TIP S 127 43.129 26.845 14.606 1.00 25.19 S ATOM 2357 OH2 TIP S 128 36.339 32.639 29.802 1.00 29.25 S ATOM 2358 OH2 TIP S 130 54.051 14.561 26.498 1.00 33.93 S ATOM 2359 OH2 TIP S 131 41.805 −4.242 5.492 1.00 33.72 S ATOM 2360 OH2 TIP S 133 38.873 25.163 36.697 1.00 30.69 S ATOM 2361 OH2 TIP S 134 28.777 8.553 25.307 1.00 31.43 S ATOM 2362 OH2 TIP S 135 53.672 10.546 −12.803 1.00 33.45 S ATOM 2363 OH2 TIP S 136 59.892 15.434 11.467 1.00 31.39 S ATOM 2364 OH2 TIP S 137 31.040 12.361 35.470 1.00 34.07 S ATOM 2365 OH2 TIP S 139 33.489 14.292 −0.598 1.00 40.68 S ATOM 2366 OH2 TIP S 140 46.918 8.748 11.662 1.00 29.23 S ATOM 2367 OH2 TIP S 141 46.297 −7.287 −9.196 1.00 42.20 S ATOM 2368 OH2 TIP S 142 58.193 6.715 −4.685 1.00 35.48 S ATOM 2369 OH2 TIP S 143 44.598 4.435 12.503 1.00 27.68 S ATOM 2370 OH2 TIP S 144 27.003 5.999 12.450 1.00 36.30 S ATOM 2371 OH2 TIP S 145 43.676 32.852 35.735 1.00 35.70 S ATOM 2372 OH2 TIP S 146 35.783 18.628 36.452 1.00 34.62 S ATOM 2373 OH2 TIP S 147 25.402 4.058 20.638 1.00 45.03 S ATOM 2374 OH2 TIP S 148 45.839 35.853 33.724 1.00 35.47 S ATOM 2375 OH2 TIP S 149 22.176 18.976 16.752 1.00 31.87 S ATOM 2376 OH2 TIP S 150 43.986 33.179 10.162 1.00 37.70 S ATOM 2377 OH2 TIP S 151 50.653 20.347 42.428 1.00 35.80 S ATOM 2378 OH2 TIP S 152 47.843 24.314 9.506 1.00 31.05 S ATOM 2379 OH2 TIP S 153 44.693 5.273 −14.175 1.00 29.90 S ATOM 2380 OH2 TIP S 155 26.560 36.851 31.684 1.00 49.29 S ATOM 2381 OH2 TIP S 156 46.867 8.019 −12.951 1.00 29.21 S ATOM 2382 OH2 TIP S 157 30.432 28.741 12.438 1.00 37.76 S ATOM 2383 OH2 TIP S 158 41.004 20.553 6.423 1.00 39.53 S ATOM 2384 OH2 TIP S 159 49.258 20.069 29.294 1.00 33.97 S ATOM 2385 OH2 TIP S 160 48.082 28.459 16.489 1.00 33.10 S ATOM 2386 OH2 TIP S 161 47.448 18.625 27.683 1.00 34.87 S ATOM 2387 OH2 TIP S 162 19.687 20.632 23.411 1.00 35.01 S ATOM 2388 OH2 TIP S 163 32.402 −1.266 22.443 1.00 37.26 S ATOM 2389 OH2 TIP S 164 39.475 33.468 33.237 1.00 35.34 S ATOM 2390 OH2 TIP S 165 44.277 18.950 5.162 1.00 45.14 S ATOM 2391 OH2 TIP S 166 34.797 30.523 10.736 1.00 47.55 S ATOM 2392 OH2 TIP S 167 46.541 3.526 −14.949 1.00 26.54 S ATOM 2393 OH2 TIP S 168 36.333 16.371 1.539 1.00 38.68 S ATOM 2394 OH2 TIP S 169 46.761 38.936 27.403 1.00 34.66 S ATOM 2395 OH2 TIP S 170 24.163 13.264 11.375 1.00 41.23 S ATOM 2396 OH2 TIP S 171 48.459 15.018 31.951 1.00 38.11 S ATOM 2397 OH2 TIP S 172 34.261 23.193 40.004 1.00 48.96 S ATOM 2398 OH2 TIP S 173 45.924 −0.026 13.224 1.00 39.55 S ATOM 2399 OH2 TIP S 175 41.384 37.389 32.543 1.00 40.74 S ATOM 2400 OH2 TIP S 177 49.394 35.312 27.150 1.00 44.33 S ATOM 2401 OH2 TIP S 178 29.066 29.942 34.359 1.00 41.46 S ATOM 2402 OH2 TIP S 180 49.354 19.467 7.273 1.00 34.56 S ATOM 2403 OH2 TIP S 181 25.298 17.029 31.863 1.00 47.74 S ATOM 2404 OH2 TIP S 182 37.071 25.027 4.669 1.00 43.87 S ATOM 2405 OH2 TIP S 183 22.581 7.487 18.691 1.00 41.75 S ATOM 2406 OH2 TIP S 184 32.269 7.011 −1.891 1.00 48.84 S ATOM 2407 OH2 TIP S 185 48.234 0.494 6.833 1.00 48.16 S ATOM 2408 OH2 TIP S 187 20.008 14.658 19.211 1.00 45.27 S ATOM 2409 OH2 TIP S 188 49.341 22.698 42.272 1.00 42.20 S ATOM 2410 OH2 TIP S 190 61.292 18.260 −8.097 1.00 45.21 S ATOM 2411 OH2 TIP S 191 28.152 10.606 2.819 1.00 40.38 S ATOM 2412 OH2 TIP S 192 25.626 12.619 23.191 1.00 34.27 S ATOM 2413 OH2 TIP S 193 59.876 11.603 1.216 1.00 46.54 S ATOM 2414 OH2 TIP S 194 57.592 21.183 −10.646 1.00 45.82 S ATOM 2415 OH2 TIP S 195 31.509 36.649 21.499 1.00 38.73 S ATOM 2416 OH2 TIP S 197 50.270 −1.543 −6.136 1.00 42.66 S ATOM 2417 OH2 TIP S 198 24.467 8.729 13.088 1.00 42.78 S ATOM 2418 OH2 TIP S 199 38.098 8.699 25.759 1.00 32.80 S ATOM 2419 OH2 TIP S 200 57.831 11.358 −13.255 1.00 45.31 S ATOM 2420 OH2 TIP S 201 23.888 22.328 30.524 1.00 37.12 S ATOM 2421 OH2 TIP S 202 47.691 26.068 37.666 1.00 37.92 S ATOM 2422 OH2 TIP S 203 38.653 7.070 29.307 1.00 50.54 S ATOM 2423 OH2 TIP S 206 44.424 27.583 2.092 1.00 53.50 S ATOM 2424 OH2 TIP S 212 22.258 2.296 17.948 1.00 47.38 S ATOM 2425 OH2 TIP S 214 19.843 17.943 23.303 1.00 30.36 S ATOM 2426 OH2 TIP S 216 27.647 11.344 24.681 1.00 31.32 S ATOM 2427 OH2 TIP S 217 37.953 7.817 −9.284 1.00 45.97 S ATOM 2428 OH2 TIP S 218 33.845 34.040 12.124 1.00 38.11 S ATOM 2429 OH2 TIP S 219 58.484 15.269 13.717 1.00 38.26 S ATOM 2430 OH2 TIP S 220 48.526 40.920 26.583 1.00 35.23 S ATOM 2431 OH2 TIP S 222 52.094 21.184 38.122 1.00 29.86 S ATOM 2432 OH2 TIP S 223 36.889 5.881 3.281 1.00 37.63 S ATOM 2433 OH2 TIP S 224 47.642 −1.401 −10.684 1.00 34.89 S ATOM 2434 OH2 TIP S 226 47.284 2.916 19.133 1.00 34.10 S ATOM 2435 OH2 TIP S 227 42.468 4.463 −15.039 1.00 37.98 S ATOM 2436 OH2 TIP S 228 19.169 22.832 21.831 1.00 41.57 S ATOM 2437 OH2 TIP S 231 57.592 12.689 14.880 1.00 50.22 S ATOM 2438 OH2 TIP S 232 27.102 9.176 5.655 1.00 40.57 S ATOM 2439 OH2 TIP S 233 58.618 9.072 −11.925 1.00 50.71 S ATOM 2440 OH2 TIP S 234 22.822 25.342 19.945 1.00 34.93 S ATOM 2441 OH2 TIP S 236 24.831 32.218 28.901 1.00 37.69 S ATOM 2442 OH2 TIP S 237 20.045 10.774 16.992 1.00 39.57 S ATOM 2443 OH2 TIP S 238 58.019 19.850 15.679 1.00 41.42 S ATOM 2444 OH2 TIP S 239 19.490 20.949 26.114 1.00 34.55 S ATOM 2445 OH2 TIP S 240 61.187 26.377 7.346 1.00 39.68 S ATOM 2446 OH2 TIP S 241 33.680 38.342 19.389 1.00 48.93 S ATOM 2447 OH2 TIP S 242 51.539 31.612 10.881 1.00 55.65 S ATOM 2448 OH2 TIP S 244 25.872 14.431 30.404 1.00 46.69 S ATOM 2449 OH2 TIP S 248 37.332 5.849 9.544 1.00 43.81 S ATOM 2450 OH2 TIP S 250 39.087 −1.293 −9.655 1.00 42.96 S ATOM 2451 OH2 TIP S 258 23.938 30.000 30.010 1.00 38.89 S ATOM 2452 OH2 TIP S 259 24.949 29.749 32.578 1.00 40.17 S ATOM 2453 OH2 TIP S 260 32.111 17.986 1.918 1.00 48.36 S ATOM 2454 OH2 TIP S 266 21.404 12.876 25.603 1.00 57.17 S ATOM 2455 OH2 TIP S 269 35.425 36.767 12.550 1.00 30.70 S ATOM 2456 OH2 TIP S 270 52.438 25.529 30.131 1.00 44.85 S ATOM 2457 OH2 TIP S 271 53.299 20.156 36.003 1.00 37.15 S ATOM 2458 OH2 TIP S 272 50.914 6.919 23.723 1.00 43.29 S ATOM 2459 OH2 TIP S 274 31.578 30.795 11.014 1.00 50.15 S ATOM 2460 OH2 TIP S 275 26.341 7.243 22.447 1.00 39.40 S ATOM 2461 OH2 TIP S 276 60.392 18.195 10.235 1.00 37.91 S ATOM 2462 OH2 TIP S 277 47.355 −9.081 −10.821 1.00 48.18 S ATOM 2463 OH2 TIP S 279 41.304 6.175 −16.647 1.00 38.12 S ATOM 2464 OH2 TIP S 282 33.299 21.620 37.881 1.00 46.29 S ATOM 2465 OH2 TIP S 283 56.469 26.112 −8.575 1.00 43.71 S ATOM 2466 OH2 TIP S 287 48.382 26.573 7.246 1.00 41.43 S ATOM 2467 OH2 TIP S 288 56.240 7.245 −11.331 1.00 41.79 S ATOM 2468 OH2 TIP S 290 49.060 14.978 28.166 1.00 37.03 S ATOM 2469 OH2 TIP S 291 37.095 44.270 26.442 1.00 45.08 S ATOM 2470 OH2 TIP S 292 47.814 −0.384 −13.299 1.00 48.60 S ATOM 2471 OH2 TIP S 297 58.081 2.784 −7.841 1.00 41.89 S ATOM 2472 OH2 TIP S 298 36.447 45.321 18.644 1.00 54.91 S ATOM 2473 OH2 TIP S 299 49.029 23.328 1.767 1.00 30.55 S ATOM 2474 OH2 TIP S 301 24.375 13.771 8.634 1.00 48.47 S ATOM 2475 OH2 TIP S 303 47.904 36.798 28.653 1.00 35.76 S ATOM 2476 OH2 TIP S 305 51.156 40.821 27.172 1.00 43.59 S ATOM 2477 OH2 TIP S 306 32.943 28.917 35.227 1.00 42.60 S ATOM 2478 OH2 TIP S 307 58.462 28.373 6.251 1.00 46.15 S ATOM 2479 OH2 TIP S 308 41.964 30.940 36.712 1.00 48.26 S ATOM 2480 OH2 TIP S 313 51.176 −1.922 −3.336 1.00 50.61 S ATOM 2481 OH2 TIP S 1001 21.319 36.868 23.805 1.00 36.97 S ATOM 2482 OH2 TIP S 1002 48.880 32.620 27.617 1.00 44.40 S ATOM 2483 OH2 TIP S 1003 61.880 19.473 11.767 1.00 45.49 S ATOM 2484 OH2 TIP S 1004 52.770 21.424 26.815 1.00 24.43 S ATOM 2485 OH2 TIP S 1005 35.373 29.094 36.197 1.00 35.97 S ATOM 2486 OH2 TIP S 1006 40.815 −6.636 4.389 1.00 43.15 S ATOM 2487 OH2 TIP S 1007 44.953 1.286 11.272 1.00 49.45 S ATOM 2488 OH2 TIP S 1010 21.004 16.168 27.009 1.00 48.51 S ATOM 2489 OH2 TIP S 1011 47.094 41.786 9.243 1.00 50.10 S ATOM 2490 OH2 TIP S 1012 32.479 2.978 14.158 1.00 49.47 S ATOM 2491 O12 GLC G 1 48.557 11.372 −12.279 1.00 40.72 G ATOM 2492 C11 GLC G 1 48.836 12.133 −11.097 1.00 38.05 G ATOM 2493 C13 GLC G 1 49.266 13.554 −11.476 1.00 38.09 G ATOM 2494 O14 GLC G 1 49.559 14.299 −10.292 1.00 33.99 G ATOM 2495 C15 GLC G 1 48.150 14.257 −12.257 1.00 37.32 G ATOM 2496 O16 GLC G 1 48.574 15.582 −12.604 1.00 36.74 G ATOM 2497 O12 GLC G 2 40.114 −6.634 −6.562 1.00 33.52 G ATOM 2498 C11 GLC G 2 38.967 −6.592 −7.404 1.00 31.05 G ATOM 2499 C13 GLC G 2 37.712 −6.417 −6.552 1.00 31.56 G ATOM 2500 O14 GLC G 2 36.554 −6.406 −7.389 1.00 30.70 G ATOM 2501 C15 GLC G 2 37.792 −5.109 −5.761 1.00 30.03 G ATOM 2502 O16 GLC G 2 36.609 −4.961 −4.975 1.00 29.66 G ATOM 2503 O12 GLC G 3 44.030 8.243 −13.470 1.00 37.90 G ATOM 2504 C11 GLC G 3 43.950 9.648 −13.690 1.00 38.47 G ATOM 2505 C13 GLC G 3 42.747 9.974 −14.579 1.00 39.52 G ATOM 2506 O14 GLC G 3 41.551 9.526 −13.942 1.00 39.39 G ATOM 2507 C15 GLC G 3 42.878 9.280 −15.934 1.00 41.43 G ATOM 2508 O16 GLC G 3 41.736 9.613 −16.731 1.00 40.78 G ATOM 2509 O12 GLC G 5 40.556 1.005 2.289 1.00 45.25 G ATOM 2510 C11 GLC G 5 40.966 2.332 1.960 1.00 40.56 G ATOM 2511 C13 GLC G 5 40.187 3.327 2.814 1.00 40.36 G ATOM 2512 O14 GLC G 5 38.791 3.169 2.572 1.00 40.71 G ATOM 2513 C15 GLC G 5 40.619 4.751 2.464 1.00 40.04 G ATOM 2514 O16 GLC G 5 39.885 5.681 3.256 1.00 36.89 G ATOM 2515 O12 GLC G 6 36.951 22.702 40.046 1.00 63.04 G ATOM 2516 C11 GLC G 6 37.592 21.583 39.422 1.00 62.46 G ATOM 2517 C13 GLC G 6 38.104 21.978 38.030 1.00 61.14 G ATOM 2518 O14 GLC G 6 39.034 23.054 38.168 1.00 61.72 G ATOM 2519 C15 GLC G 6 36.948 22.429 37.126 1.00 60.51 G ATOM 2520 O16 GLC G 6 35.992 21.372 36.960 1.00 58.61 G ATOM 2521 O12 GLC G 7 37.316 0.281 14.299 1.00 73.45 G ATOM 2522 C11 GLC G 7 37.655 −0.758 15.222 1.00 72.78 G ATOM 2523 C13 GLC G 7 36.592 −1.856 15.157 1.00 72.98 G ATOM 2524 O14 GLC G 7 35.320 −1.299 15.498 1.00 73.88 G ATOM 2525 C15 GLC G 7 36.924 −2.989 16.134 1.00 73.66 G ATOM 2526 O16 GLC G 7 36.972 −2.493 17.478 1.00 75.38 G ATOM 2527 O12 GLC G 8 51.921 21.898 5.908 1.00 62.51 G ATOM 2528 C11 GLC G 8 52.447 20.871 5.063 1.00 63.42 G ATOM 2529 C13 GLC G 8 51.476 20.597 3.908 1.00 64.28 G ATOM 2530 O14 GLC G 8 51.297 21.794 3.150 1.00 66.28 G ATOM 2531 C15 GLC G 8 50.121 20.137 4.448 1.00 64.49 G ATOM 2532 O16 GLC G 8 49.233 19.886 3.357 1.00 64.01 G ATOM 2533 O12 GLC G 10 36.044 37.499 29.523 1.00 56.89 G ATOM 2534 C11 GLC G 10 35.164 36.645 30.259 1.00 56.97 G ATOM 2535 C13 GLC G 10 33.849 36.489 29.494 1.00 56.11 G ATOM 2536 O14 GLC G 10 33.248 37.772 29.308 1.00 56.44 G ATOM 2537 C15 GLC G 10 32.900 35.580 30.277 1.00 55.84 G ATOM 2538 O16 GLC G 10 31.674 35.442 29.557 1.00 55.39 G ATOM 2539 O3G ATP N 1 46.280 25.658 5.170 1.00 51.49 N ATOM 2540 PG ATP N 1 46.464 25.053 3.691 1.00 52.22 N ATOM 2541 O1G ATP N 1 47.406 23.911 3.763 1.00 51.41 N ATOM 2542 O2G ATP N 1 46.794 26.182 2.784 1.00 52.07 N ATOM 2543 O3B ATP N 1 44.976 24.513 3.344 1.00 51.01 N ATOM 2544 PB ATP N 1 44.560 22.969 3.605 1.00 50.20 N ATOM 2545 O1B ATP N 1 43.083 22.898 3.669 1.00 49.41 N ATOM 2546 O2B ATP N 1 45.345 22.474 4.766 1.00 50.34 N ATOM 2547 O3A ATP N 1 45.070 22.231 2.255 1.00 47.77 N ATOM 2548 PA ATP N 1 45.075 20.613 2.121 1.00 42.84 N ATOM 2549 O1A ATP N 1 45.547 20.291 0.754 1.00 43.81 N ATOM 2550 O2A ATP N 1 45.807 20.035 3.270 1.00 45.03 N ATOM 2551 O5* ATP N 1 43.516 20.223 2.245 1.00 41.73 N ATOM 2552 C5* ATP N 1 42.528 20.925 1.489 1.00 37.57 N ATOM 2553 C4* ATP N 1 41.127 20.379 1.776 1.00 39.45 N ATOM 2554 O4* ATP N 1 40.907 19.024 1.279 1.00 37.72 N ATOM 2555 C3* ATP N 1 40.777 20.321 3.251 1.00 38.48 N ATOM 2556 O3* ATP N 1 40.360 21.615 3.697 1.00 40.42 N ATOM 2557 C2* ATP N 1 39.608 19.374 3.270 1.00 37.58 N ATOM 2558 O2* ATP N 1 38.410 20.076 2.924 1.00 35.98 N ATOM 2559 C1* ATP N 1 39.939 18.346 2.173 1.00 35.55 N ATOM 2560 N9 ATP N 1 40.628 17.156 2.747 1.00 31.76 N ATOM 2561 C8 ATP N 1 41.864 17.126 3.274 1.00 30.49 N ATOM 2562 N7 ATP N 1 42.143 15.877 3.667 1.00 29.75 N ATOM 2563 C5 ATP N 1 41.088 15.118 3.390 1.00 27.49 N ATOM 2564 C4 ATP N 1 40.125 15.925 2.810 1.00 30.02 N ATOM 2565 N3 ATP N 1 38.937 15.389 2.431 1.00 27.11 N ATOM 2566 C2 ATP N 1 38.679 14.085 2.615 1.00 25.62 N ATOM 2567 N1 ATP N 1 39.597 13.283 3.175 1.00 21.76 N ATOM 2568 C6 ATP N 1 40.800 13.768 3.571 1.00 23.90 N ATOM 2569 N6 ATP N 1 41.698 12.964 4.127 1.00 21.94 N ATOM 2570 S SO4 I 1 58.680 8.493 −0.639 1.00 56.05 I ATOM 2571 O1 SO4 I 1 57.956 7.875 0.483 1.00 58.83 I ATOM 2572 O2 SO4 I 1 57.886 9.607 −1.188 1.00 57.04 I ATOM 2573 O3 SO4 I 1 58.906 7.478 −1.683 1.00 57.47 I ATOM 2574 O4 SO4 I 1 59.976 9.008 −0.156 1.00 57.51 I ATOM 2575 S SO4 I 2 39.339 4.855 7.057 1.00 84.24 I ATOM 2576 O1 SO4 I 2 39.390 6.175 7.711 1.00 85.02 I ATOM 2577 O2 SO4 I 2 40.101 4.897 5.797 1.00 84.75 I ATOM 2578 O3 SO4 I 2 37.936 4.506 6.766 1.00 84.94 I ATOM 2579 O4 SO4 I 2 39.931 3.842 7.954 1.00 84.44 I ATOM 2580 S SO4 I 3 38.987 −2.256 3.310 1.00 58.58 I ATOM 2581 O1 SO4 I 3 37.734 −1.675 3.827 1.00 59.11 I ATOM 2582 O2 SO4 I 3 39.460 −1.454 2.172 1.00 59.91 I ATOM 2583 O3 SO4 I 3 38.743 −3.640 2.866 1.00 60.97 I ATOM 2584 O4 SO4 I 3 40.014 −2.260 4.369 1.00 59.58 I ATOM 2585 S SO4 I 4 34.397 5.289 30.981 1.00 64.34 I ATOM 2586 O1 SO4 I 4 33.627 6.528 30.742 1.00 60.43 I ATOM 2587 O2 SO4 I 4 34.337 4.427 29.782 1.00 60.11 I ATOM 2588 O3 SO4 I 4 33.816 4.572 32.133 1.00 64.39 I ATOM 2589 O4 SO4 I 4 35.806 5.626 31.277 1.00 63.55 I ATOM 2590 S SO4 I 5 55.074 −6.984 −3.711 1.00 75.40 I ATOM 2591 O1 SO4 I 5 54.657 −7.518 −2.399 1.00 74.66 I ATOM 2592 O2 SO4 I 5 54.209 −5.845 −4.065 1.00 74.96 I ATOM 2593 O3 SO4 I 5 54.950 −8.034 −4.742 1.00 74.22 I ATOM 2594 O4 SO4 I 5 56.477 −6.532 −3.633 1.00 75.15 I ATOM 2595 O2 PO4 P 100 57.362 24.998 13.149 1.00 66.76 P ATOM 2596 O3 PO4 P 100 59.399 26.166 13.761 1.00 66.89 P ATOM 2597 O4 PO4 P 100 57.761 25.606 15.462 1.00 67.43 P ATOM 2598 O1 PO4 P 100 57.264 27.325 13.818 1.00 65.91 P ATOM 2599 P PO4 P 100 57.947 26.025 14.048 1.00 66.69 P END

Example 4 Co-Ordinates for the Dimer of the PDK1 Fragment, without Alternate Side Chains

Chain A is the molecule for which co-ordinates are given in Examples 2 and 3, and chain B is the symmetry-related molecule.

ATOM 1 CB PRO A 71 58.912 −7.251 8.216 1.00 67.78 A ATOM 2 CG PRO A 71 59.621 −6.941 9.534 1.00 69.16 A ATOM 3 C PRO A 71 59.493 −6.506 5.894 1.00 67.06 A ATOM 4 O PRO A 71 59.196 −5.318 5.766 1.00 66.66 A ATOM 5 N PRO A 71 60.984 −6.073 7.833 1.00 67.86 A ATOM 6 CD PRO A 71 60.554 −5.762 9.207 1.00 68.24 A ATOM 7 CA PRO A 71 60.040 −7.035 7.217 1.00 67.75 A ATOM 8 N PRO A 72 59.356 −7.385 4.890 1.00 66.32 A ATOM 9 CD PRO A 72 59.712 −8.816 4.898 1.00 67.17 A ATOM 10 CA PRO A 72 58.840 −6.986 3.578 1.00 65.61 A ATOM 11 CB PRO A 72 58.672 −8.321 2.858 1.00 66.47 A ATOM 12 CG PRO A 72 59.796 −9.133 3.419 1.00 67.57 A ATOM 13 C PRO A 72 57.527 −6.208 3.673 1.00 63.94 A ATOM 14 O PRO A 72 56.710 −6.451 4.561 1.00 64.11 A ATOM 15 N ALA A 73 57.341 −5.268 2.753 1.00 61.57 A ATOM 16 CA ALA A 73 56.133 −4.454 2.708 1.00 58.74 A ATOM 17 CB ALA A 73 56.438 −3.030 3.165 1.00 58.05 A ATOM 18 C ALA A 73 55.626 −4.448 1.271 1.00 56.78 A ATOM 19 O ALA A 73 56.347 −4.834 0.349 1.00 56.95 A ATOM 20 N PRO A 74 54.372 −4.024 1.057 1.00 54.15 A ATOM 21 CD PRO A 74 53.335 −3.610 2.018 1.00 53.31 A ATOM 22 CA PRO A 74 53.856 −4.003 −0.314 1.00 52.54 A ATOM 23 CB PRO A 74 52.474 −3.375 −0.148 1.00 52.86 A ATOM 24 CG PRO A 74 52.067 −3.824 1.226 1.00 52.88 A ATOM 25 C PRO A 74 54.772 −3.167 −1.204 1.00 50.08 A ATOM 26 O PRO A 74 55.559 −2.361 −0.708 1.00 49.96 A ATOM 27 N ALA A 75 54.680 −3.366 −2.514 1.00 47.58 A ATOM 28 CA ALA A 75 55.503 −2.602 −3.446 1.00 44.69 A ATOM 29 CB ALA A 75 55.312 −3.121 −4.870 1.00 46.14 A ATOM 30 C ALA A 75 55.100 −1.134 −3.371 1.00 41.55 A ATOM 31 O ALA A 75 53.947 −0.813 −3.086 1.00 41.01 A ATOM 32 N LYS A 76 56.053 −0.245 −3.619 1.00 38.31 A ATOM 33 CA LYS A 76 55.781 1.184 −3.588 1.00 35.72 A ATOM 34 CB LYS A 76 57.053 1.957 −3.930 1.00 37.70 A ATOM 35 CG LYS A 76 57.123 3.356 −3.350 1.00 40.99 A ATOM 36 CD LYS A 76 57.262 3.316 −1.836 1.00 40.04 A ATOM 37 CE LYS A 76 57.511 4.705 −1.277 1.00 42.08 A ATOM 38 NZ LYS A 76 57.681 4.695 0.202 1.00 42.99 A ATOM 39 C LYS A 76 54.708 1.467 −4.638 1.00 32.65 A ATOM 40 O LYS A 76 54.814 1.005 −5.770 1.00 31.41 A ATOM 41 N LYS A 77 53.668 2.207 −4.270 1.00 28.59 A ATOM 42 CA LYS A 77 52.619 2.517 −5.232 1.00 25.72 A ATOM 43 CB LYS A 77 51.316 2.865 −4.509 1.00 26.22 A ATOM 44 CG LYS A 77 50.796 1.731 −3.631 1.00 27.15 A ATOM 45 CD LYS A 77 49.487 2.089 −2.967 1.00 26.80 A ATOM 46 CE LYS A 77 49.136 1.091 −1.870 1.00 27.31 A ATOM 47 NZ LYS A 77 48.998 −0.296 −2.380 1.00 27.17 A ATOM 48 C LYS A 77 53.053 3.668 −6.137 1.00 24.67 A ATOM 49 O LYS A 77 54.010 4.377 −5.829 1.00 21.60 A ATOM 50 N ARG A 78 52.351 3.838 −7.254 1.00 23.66 A ATOM 51 CA ARG A 78 52.662 4.897 −8.211 1.00 26.14 A ATOM 52 CB ARG A 78 53.574 4.344 −9.318 1.00 28.57 A ATOM 53 CG ARG A 78 53.017 3.139 −10.050 1.00 34.78 A ATOM 54 CD ARG A 78 54.092 2.465 −10.896 1.00 40.96 A ATOM 55 NE ARG A 78 53.560 1.364 −11.700 1.00 48.93 A ATOM 56 CZ ARG A 78 52.985 0.270 −11.203 1.00 52.58 A ATOM 57 NH1 ARG A 78 52.860 0.113 −9.889 1.00 54.60 A ATOM 58 NH2 ARG A 78 52.530 −0.672 −12.022 1.00 54.09 A ATOM 59 C ARG A 78 51.382 5.488 −8.803 1.00 23.76 A ATOM 60 O ARG A 78 50.311 4.888 −8.706 1.00 24.25 A ATOM 61 N PRO A 79 51.475 6.676 −9.428 1.00 21.76 A ATOM 62 CD PRO A 79 52.691 7.475 −9.668 1.00 20.82 A ATOM 63 CA PRO A 79 50.301 7.325 −10.021 1.00 21.96 A ATOM 64 CB PRO A 79 50.910 8.481 −10.816 1.00 22.27 A ATOM 65 CG PRO A 79 52.124 8.831 −10.014 1.00 22.12 A ATOM 66 C PRO A 79 49.446 6.413 −10.903 1.00 22.86 A ATOM 67 O PRO A 79 48.213 6.461 −10.842 1.00 20.52 A ATOM 68 N GLU A 80 50.103 5.586 −11.714 1.00 21.87 A ATOM 69 CA GLU A 80 49.403 4.685 −12.628 1.00 22.99 A ATOM 70 CB GLU A 80 50.393 3.994 −13.571 1.00 25.24 A ATOM 71 CG GLU A 80 51.230 2.907 −12.925 1.00 28.75 A ATOM 72 CD GLU A 80 52.157 2.224 −13.913 1.00 31.99 A ATOM 73 OE1 GLU A 80 53.072 2.897 −14.433 1.00 34.34 A ATOM 74 OE2 GLU A 80 51.969 1.015 −14.172 1.00 32.83 A ATOM 75 C GLU A 80 48.556 3.631 −11.912 1.00 22.09 A ATOM 76 O GLU A 80 47.692 3.013 −12.530 1.00 22.37 A ATOM 77 N ASP A 81 48.804 3.413 −10.622 1.00 19.97 A ATOM 78 CA ASP A 81 48.026 2.423 −9.874 1.00 19.93 A ATOM 79 CB ASP A 81 48.736 2.029 −8.571 1.00 21.19 A ATOM 80 CG ASP A 81 50.089 1.380 −8.807 1.00 22.46 A ATOM 81 OD1 ASP A 81 50.195 0.554 −9.731 1.00 24.22 A ATOM 82 OD2 ASP A 81 51.043 1.685 −8.058 1.00 23.33 A ATOM 83 C ASP A 81 46.652 2.975 −9.518 1.00 20.85 A ATOM 84 O ASP A 81 45.793 2.246 −9.015 1.00 19.96 A ATOM 85 N PHE A 82 46.445 4.258 −9.804 1.00 18.91 A ATOM 86 CA PHE A 82 45.200 4.934 −9.465 1.00 19.30 A ATOM 87 CB PHE A 82 45.475 6.027 −8.427 1.00 18.43 A ATOM 88 CG PHE A 82 46.134 5.531 −7.175 1.00 18.01 A ATOM 89 CD1 PHE A 82 45.371 5.136 −6.084 1.00 17.19 A ATOM 90 CD2 PHE A 82 47.520 5.460 −7.086 1.00 18.99 A ATOM 91 CE1 PHE A 82 45.977 4.676 −4.918 1.00 17.12 A ATOM 92 CE2 PHE A 82 48.137 5.000 −5.925 1.00 19.64 A ATOM 93 CZ PHE A 82 47.361 4.607 −4.838 1.00 18.00 A ATOM 94 C PHE A 82 44.476 5.596 −10.621 1.00 20.81 A ATOM 95 O PHE A 82 45.066 5.933 −11.649 1.00 20.34 A ATOM 96 N LYS A 83 43.182 5.792 −10.411 1.00 19.80 A ATOM 97 CA LYS A 83 42.321 6.478 −11.353 1.00 21.65 A ATOM 98 CB LYS A 83 41.096 5.625 −11.687 1.00 22.02 A ATOM 99 CG LYS A 83 40.062 6.326 −12.550 1.00 28.93 A ATOM 100 CD LYS A 83 38.974 5.355 −12.981 1.00 34.20 A ATOM 101 CE LYS A 83 37.909 6.042 −13.824 1.00 38.10 A ATOM 102 NZ LYS A 83 37.179 7.086 −13.043 1.00 43.33 A ATOM 103 C LYS A 83 41.913 7.702 −10.541 1.00 20.74 A ATOM 104 O LYS A 83 41.084 7.606 −9.635 1.00 20.98 A ATOM 105 N PHE A 84 42.513 8.848 −10.835 1.00 19.99 A ATOM 106 CA PHE A 84 42.188 10.049 −10.083 1.00 18.63 A ATOM 107 CB PHE A 84 43.279 11.103 −10.258 1.00 18.95 A ATOM 108 CG PHE A 84 44.571 10.741 −9.587 1.00 17.68 A ATOM 109 CD1 PHE A 84 45.498 9.926 −10.224 1.00 18.16 A ATOM 110 CD2 PHE A 84 44.843 11.183 −8.299 1.00 19.66 A ATOM 111 CE1 PHE A 84 46.676 9.556 −9.589 1.00 18.09 A ATOM 112 CE2 PHE A 84 46.021 10.816 −7.653 1.00 18.89 A ATOM 113 CZ PHE A 84 46.936 10.002 −8.301 1.00 17.33 A ATOM 114 C PHE A 84 40.834 10.617 −10.460 1.00 19.69 A ATOM 115 O PHE A 84 40.391 10.489 −11.601 1.00 20.72 A ATOM 116 N GLY A 85 40.178 11.233 −9.484 1.00 16.80 A ATOM 117 CA GLY A 85 38.872 11.810 −9.716 1.00 17.73 A ATOM 118 C GLY A 85 38.819 13.280 −9.346 1.00 18.75 A ATOM 119 O GLY A 85 39.740 14.043 −9.650 1.00 18.45 A ATOM 120 N LYS A 86 37.753 13.673 −8.659 1.00 16.00 A ATOM 121 CA LYS A 86 37.571 15.064 −8.278 1.00 18.26 A ATOM 122 CB LYS A 86 36.133 15.302 −7.812 1.00 19.00 A ATOM 123 CG LYS A 86 35.793 14.660 −6.481 1.00 21.55 A ATOM 124 CD LYS A 86 34.368 14.981 −6.066 1.00 26.48 A ATOM 125 CE LYS A 86 33.994 14.239 −4.793 1.00 31.92 A ATOM 126 NZ LYS A 86 32.568 14.457 −4.412 1.00 35.36 A ATOM 127 C LYS A 86 38.523 15.571 −7.202 1.00 18.57 A ATOM 128 O LYS A 86 39.045 14.807 −6.385 1.00 16.77 A ATOM 129 N ILE A 87 38.737 16.881 −7.227 1.00 17.88 A ATOM 130 CA ILE A 87 39.577 17.554 −6.256 1.00 18.26 A ATOM 131 CB ILE A 87 39.994 18.952 −6.772 1.00 19.60 A ATOM 132 CG2 ILE A 87 40.593 19.786 −5.628 1.00 18.73 A ATOM 133 CG1 ILE A 87 40.968 18.786 −7.945 1.00 21.16 A ATOM 134 CD1 ILE A 87 41.412 20.087 −8.588 1.00 25.26 A ATOM 135 C ILE A 87 38.731 17.709 −4.997 1.00 19.67 A ATOM 136 O ILE A 87 37.628 18.249 −5.052 1.00 20.41 A ATOM 137 N LEU A 88 39.240 17.229 −3.867 1.00 19.15 A ATOM 138 CA LEU A 88 38.508 17.324 −2.611 1.00 20.68 A ATOM 139 CB LEU A 88 38.870 16.151 −1.700 1.00 19.97 A ATOM 140 CG LEU A 88 38.529 14.759 −2.237 1.00 19.24 A ATOM 141 CD1 LEU A 88 39.090 13.692 −1.311 1.00 21.41 A ATOM 142 CD2 LEU A 88 37.029 14.622 −2.359 1.00 18.84 A ATOM 143 C LEU A 88 38.815 18.632 −1.901 1.00 23.11 A ATOM 144 O LEU A 88 37.999 19.146 −1.139 1.00 25.10 A ATOM 145 N GLY A 89 39.997 19.174 −2.149 1.00 24.09 A ATOM 146 CA GLY A 89 40.367 20.418 −1.507 1.00 24.27 A ATOM 147 C GLY A 89 41.658 20.954 −2.078 1.00 25.47 A ATOM 148 O GLY A 89 42.445 20.202 −2.666 1.00 22.19 A ATOM 149 N GLU A 90 41.870 22.254 −1.906 1.00 26.22 A ATOM 150 CA GLU A 90 43.064 22.924 −2.404 1.00 29.96 A ATOM 151 CB GLU A 90 42.698 23.814 −3.596 1.00 30.75 A ATOM 152 CG GLU A 90 42.267 23.038 −4.831 1.00 34.32 A ATOM 153 CD GLU A 90 41.711 23.930 −5.927 1.00 38.27 A ATOM 154 OE1 GLU A 90 40.590 24.456 −5.764 1.00 40.57 A ATOM 155 OE2 GLU A 90 42.398 24.110 −6.952 1.00 40.90 A ATOM 156 C GLU A 90 43.711 23.768 −1.313 1.00 30.68 A ATOM 157 O GLU A 90 43.049 24.574 −0.668 1.00 32.83 A ATOM 158 N GLY A 91 45.006 23.566 −1.104 1.00 29.66 A ATOM 159 CA GLY A 91 45.724 24.332 −0.104 1.00 29.40 A ATOM 160 C GLY A 91 46.795 25.151 −0.798 1.00 29.98 A ATOM 161 O GLY A 91 46.894 25.130 −2.028 1.00 28.16 A ATOM 162 N SER A 92 47.605 25.870 −0.029 1.00 28.30 A ATOM 163 CA SER A 92 48.653 26.681 −0.633 1.00 30.50 A ATOM 164 CB SER A 92 49.165 27.717 0.370 1.00 32.43 A ATOM 165 OG SER A 92 49.520 27.099 1.593 1.00 40.94 A ATOM 166 C SER A 92 49.815 25.843 −1.164 1.00 29.77 A ATOM 167 O SER A 92 50.456 26.221 −2.143 1.00 30.46 A ATOM 168 N PHE A 93 50.087 24.703 −0.536 1.00 27.65 A ATOM 169 CA PHE A 93 51.185 23.855 −0.995 1.00 26.34 A ATOM 170 CB PHE A 93 52.281 23.785 0.068 1.00 27.95 A ATOM 171 CG PHE A 93 52.861 25.117 0.406 1.00 31.06 A ATOM 172 CD1 PHE A 93 52.283 25.909 1.392 1.00 29.96 A ATOM 173 CD2 PHE A 93 53.949 25.613 −0.308 1.00 31.38 A ATOM 174 CE1 PHE A 93 52.779 27.181 1.665 1.00 32.69 A ATOM 175 CE2 PHE A 93 54.452 26.883 −0.044 1.00 32.63 A ATOM 176 CZ PHE A 93 53.864 27.670 0.945 1.00 31.81 A ATOM 177 C PHE A 93 50.759 22.445 −1.365 1.00 25.39 A ATOM 178 O PHE A 93 51.601 21.559 −1.522 1.00 24.59 A ATOM 179 N SER A 94 49.457 22.235 −1.519 1.00 23.63 A ATOM 180 CA SER A 94 48.965 20.912 −1.860 1.00 21.43 A ATOM 181 CB SER A 94 49.017 20.013 −0.628 1.00 21.42 A ATOM 182 OG SER A 94 48.091 20.475 0.340 1.00 21.19 A ATOM 183 C SER A 94 47.539 20.925 −2.378 1.00 19.82 A ATOM 184 O SER A 94 46.795 21.882 −2.173 1.00 18.76 A ATOM 185 N THR A 95 47.174 19.832 −3.038 1.00 19.38 A ATOM 186 CA THR A 95 45.840 19.637 −3.580 1.00 17.98 A ATOM 187 CB THR A 95 45.818 19.818 −5.110 1.00 19.25 A ATOM 188 OG1 THR A 95 46.196 21.162 −5.434 1.00 22.04 A ATOM 189 CG2 THR A 95 44.421 19.549 −5.661 1.00 17.61 A ATOM 190 C THR A 95 45.455 18.201 −3.243 1.00 18.61 A ATOM 191 O THR A 95 46.212 17.264 −3.524 1.00 17.10 A ATOM 192 N VAL A 96 44.295 18.024 −2.623 1.00 16.53 A ATOM 193 CA VAL A 96 43.845 16.685 −2.266 1.00 16.05 A ATOM 194 CB VAL A 96 43.170 16.672 −0.886 1.00 16.32 A ATOM 195 CG1 VAL A 96 42.741 15.249 −0.532 1.00 18.02 A ATOM 196 CG2 VAL A 96 44.145 17.206 0.168 1.00 16.69 A ATOM 197 C VAL A 96 42.875 16.207 −3.335 1.00 16.42 A ATOM 198 O VAL A 96 41.906 16.892 −3.665 1.00 16.47 A ATOM 199 N VAL A 97 43.157 15.033 −3.888 1.00 16.80 A ATOM 200 CA VAL A 97 42.338 14.471 −4.949 1.00 16.72 A ATOM 201 CB VAL A 97 43.153 14.354 −6.255 1.00 18.43 A ATOM 202 CG1 VAL A 97 42.249 13.927 −7.404 1.00 19.69 A ATOM 203 CG2 VAL A 97 43.831 15.685 −6.569 1.00 17.84 A ATOM 204 C VAL A 97 41.812 13.091 −4.583 1.00 16.77 A ATOM 205 O VAL A 97 42.532 12.270 −4.014 1.00 17.13 A ATOM 206 N LEU A 98 40.545 12.845 −4.895 1.00 16.62 A ATOM 207 CA LEU A 98 39.947 11.548 −4.624 1.00 17.04 A ATOM 208 CB LEU A 98 38.424 11.633 −4.743 1.00 16.89 A ATOM 209 CG LEU A 98 37.635 10.342 −4.508 1.00 19.46 A ATOM 210 CD1 LEU A 98 37.990 9.762 −3.146 1.00 20.07 A ATOM 211 CD2 LEU A 98 36.143 10.627 −4.588 1.00 17.93 A ATOM 212 C LEU A 98 40.512 10.597 −5.677 1.00 17.38 A ATOM 213 O LEU A 98 40.527 10.920 −6.863 1.00 18.60 A ATOM 214 N ALA A 99 40.995 9.438 −5.246 1.00 17.13 A ATOM 215 CA ALA A 99 41.570 8.466 −6.168 1.00 18.42 A ATOM 216 CB ALA A 99 43.090 8.524 −6.105 1.00 14.76 A ATOM 217 C ALA A 99 41.102 7.055 −5.848 1.00 21.40 A ATOM 218 O ALA A 99 40.941 6.691 −4.679 1.00 22.52 A ATOM 219 N ARG A 100 40.878 6.261 −6.888 1.00 19.77 A ATOM 220 CA ARG A 100 40.459 4.884 −6.693 1.00 20.85 A ATOM 221 CB ARG A 100 39.202 4.585 −7.518 1.00 24.22 A ATOM 222 CG ARG A 100 38.608 3.205 −7.256 1.00 31.78 A ATOM 223 CD ARG A 100 37.326 2.979 −8.048 1.00 36.24 A ATOM 224 NE ARG A 100 36.213 3.818 −7.594 1.00 41.40 A ATOM 225 CZ ARG A 100 35.566 3.662 −6.439 1.00 42.05 A ATOM 226 NH1 ARG A 100 35.912 2.696 −5.598 1.00 40.67 A ATOM 227 NH2 ARG A 100 34.559 4.468 −6.128 1.00 43.65 A ATOM 228 C ARG A 100 41.613 3.985 −7.129 1.00 18.63 A ATOM 229 O ARG A 100 42.078 4.065 −8.271 1.00 19.49 A ATOM 230 N GLU A 101 42.102 3.157 −6.212 1.00 16.43 A ATOM 231 CA GLU A 101 43.196 2.246 −6.533 1.00 16.11 A ATOM 232 CB GLU A 101 43.774 1.637 −5.248 1.00 16.79 A ATOM 233 CG GLU A 101 44.917 0.657 −5.488 1.00 16.51 A ATOM 234 CD GLU A 101 45.501 0.115 −4.200 1.00 18.20 A ATOM 235 OE1 GLU A 101 44.733 −0.081 −3.239 1.00 18.32 A ATOM 236 OE2 GLU A 101 46.725 −0.132 −4.150 1.00 17.14 A ATOM 237 C GLU A 101 42.625 1.152 −7.442 1.00 17.92 A ATOM 238 O GLU A 101 41.681 0.462 −7.069 1.00 18.02 A ATOM 239 N LEU A 102 43.198 1.002 −8.632 1.00 19.06 A ATOM 240 CA LEU A 102 42.718 0.025 −9.607 1.00 20.71 A ATOM 241 CB LEU A 102 43.569 0.097 −10.878 1.00 23.42 A ATOM 242 CG LEU A 102 43.531 1.426 −11.642 1.00 25.30 A ATOM 243 CD1 LEU A 102 44.577 1.414 −12.748 1.00 27.88 A ATOM 244 CD2 LEU A 102 42.140 1.647 −12.214 1.00 26.79 A ATOM 245 C LEU A 102 42.671 −1.418 −9.125 1.00 21.62 A ATOM 246 O LEU A 102 41.668 −2.103 −9.305 1.00 21.09 A ATOM 247 N ALA A 103 43.753 −1.874 −8.507 1.00 19.38 A ATOM 248 CA ALA A 103 43.836 −3.249 −8.035 1.00 20.87 A ATOM 249 CB ALA A 103 45.284 −3.571 −7.671 1.00 19.23 A ATOM 250 C ALA A 103 42.919 −3.629 −6.872 1.00 19.92 A ATOM 251 O ALA A 103 42.703 −4.815 −6.628 1.00 20.38 A ATOM 252 N THR A 104 42.361 −2.643 −6.175 1.00 18.12 A ATOM 253 CA THR A 104 41.517 −2.927 −5.018 1.00 17.15 A ATOM 254 CB THR A 104 42.212 −2.484 −3.717 1.00 19.54 A ATOM 255 OG1 THR A 104 42.456 −1.070 −3.773 1.00 19.26 A ATOM 256 CG2 THR A 104 43.536 −3.219 −3.529 1.00 17.02 A ATOM 257 C THR A 104 40.159 −2.247 −5.026 1.00 19.44 A ATOM 258 O THR A 104 39.259 −2.648 −4.285 1.00 18.70 A ATOM 259 N SER A 105 40.034 −1.207 −5.847 1.00 19.65 A ATOM 260 CA SER A 105 38.819 −0.400 −5.967 1.00 19.37 A ATOM 261 CB SER A 105 37.598 −1.304 −6.173 1.00 21.81 A ATOM 262 OG SER A 105 36.431 −0.539 −6.412 1.00 23.01 A ATOM 263 C SER A 105 38.644 0.447 −4.701 1.00 18.99 A ATOM 264 O SER A 105 37.602 1.070 −4.488 1.00 18.66 A ATOM 265 N ARG A 106 39.674 0.468 −3.861 1.00 16.84 A ATOM 266 CA ARG A 106 39.655 1.267 −2.634 1.00 16.21 A ATOM 267 CB ARG A 106 40.827 0.886 −1.723 1.00 16.41 A ATOM 268 CG ARG A 106 40.619 −0.367 −0.906 1.00 15.49 A ATOM 269 CD ARG A 106 41.887 −0.755 −0.170 1.00 17.43 A ATOM 270 NE ARG A 106 41.620 −1.792 0.824 1.00 20.47 A ATOM 271 CZ ARG A 106 42.548 −2.568 1.371 1.00 20.24 A ATOM 272 NH1 ARG A 106 43.821 −2.433 1.017 1.00 17.80 A ATOM 273 NH2 ARG A 106 42.198 −3.468 2.285 1.00 20.14 A ATOM 274 C ARG A 106 39.785 2.746 −2.981 1.00 17.37 A ATOM 275 O ARG A 106 40.514 3.103 −3.902 1.00 17.75 A ATOM 276 N GLU A 107 39.085 3.599 −2.240 1.00 16.06 A ATOM 277 CA GLU A 107 39.156 5.039 −2.461 1.00 20.80 A ATOM 278 CB GLU A 107 37.779 5.694 −2.337 1.00 22.93 A ATOM 279 CG GLU A 107 36.711 5.171 −3.269 1.00 30.87 A ATOM 280 CD GLU A 107 35.431 5.975 −3.148 1.00 32.40 A ATOM 281 OE1 GLU A 107 35.262 6.939 −3.923 1.00 33.74 A ATOM 282 OE2 GLU A 107 34.608 5.654 −2.263 1.00 36.00 A ATOM 283 C GLU A 107 40.053 5.678 −1.410 1.00 18.93 A ATOM 284 O GLU A 107 39.891 5.427 −0.220 1.00 19.21 A ATOM 285 N TYR A 108 40.988 6.507 −1.852 1.00 16.70 A ATOM 286 CA TYR A 108 41.883 7.209 −0.942 1.00 15.86 A ATOM 287 CB TYR A 108 43.325 6.728 −1.104 1.00 15.30 A ATOM 288 CG TYR A 108 43.593 5.328 −0.612 1.00 16.33 A ATOM 289 CD1 TYR A 108 43.765 5.066 0.746 1.00 16.36 A ATOM 290 CE1 TYR A 108 44.046 3.769 1.201 1.00 18.48 A ATOM 291 CD2 TYR A 108 43.701 4.268 −1.511 1.00 13.25 A ATOM 292 CE2 TYR A 108 43.980 2.981 −1.075 1.00 17.28 A ATOM 293 CZ TYR A 108 44.152 2.736 0.276 1.00 19.17 A ATOM 294 OH TYR A 108 44.440 1.461 0.688 1.00 19.38 A ATOM 295 C TYR A 108 41.850 8.687 −1.292 1.00 16.80 A ATOM 296 O TYR A 108 41.560 9.058 −2.431 1.00 15.22 A ATOM 297 N ALA A 109 42.132 9.528 −0.306 1.00 14.61 A ATOM 298 CA ALA A 109 42.207 10.957 −0.539 1.00 14.30 A ATOM 299 CB ALA A 109 41.671 11.726 0.661 1.00 14.78 A ATOM 300 C ALA A 109 43.713 11.136 −0.667 1.00 16.79 A ATOM 301 O ALA A 109 44.450 10.983 0.317 1.00 16.52 A ATOM 302 N ILE A 110 44.182 11.410 −1.881 1.00 14.80 A ATOM 303 CA ILE A 110 45.609 11.574 −2.093 1.00 15.80 A ATOM 304 CB ILE A 110 46.065 10.863 −3.396 1.00 16.85 A ATOM 305 CG2 ILE A 110 47.550 11.098 −3.632 1.00 16.80 A ATOM 306 CG1 ILE A 110 45.774 9.358 −3.284 1.00 17.76 A ATOM 307 CD1 ILE A 110 46.308 8.513 −4.437 1.00 16.07 A ATOM 308 C ILE A 110 46.004 13.045 −2.129 1.00 17.78 A ATOM 309 O ILE A 110 45.534 13.813 −2.976 1.00 16.24 A ATOM 310 N LYS A 111 46.846 13.435 −1.177 1.00 16.15 A ATOM 311 CA LYS A 111 47.326 14.808 −1.100 1.00 17.20 A ATOM 312 CB LYS A 111 47.700 15.176 0.344 1.00 17.41 A ATOM 313 CG LYS A 111 48.350 16.547 0.464 1.00 20.71 A ATOM 314 CD LYS A 111 48.585 16.971 1.910 1.00 24.25 A ATOM 315 CE LYS A 111 47.288 17.381 2.598 1.00 29.46 A ATOM 316 NZ LYS A 111 47.516 17.866 4.000 1.00 30.50 A ATOM 317 C LYS A 111 48.551 14.890 −1.994 1.00 16.41 A ATOM 318 O LYS A 111 49.509 14.137 −1.813 1.00 18.20 A ATOM 319 N ILE A 112 48.509 15.798 −2.963 1.00 15.87 A ATOM 320 CA ILE A 112 49.606 15.967 −3.907 1.00 17.28 A ATOM 321 CB ILE A 112 49.079 15.911 −5.358 1.00 16.43 A ATOM 322 CG2 ILE A 112 50.235 15.998 −6.341 1.00 15.12 A ATOM 323 CG1 ILE A 112 48.293 14.609 −5.565 1.00 16.82 A ATOM 324 CD1 ILE A 112 47.580 14.511 −6.904 1.00 18.47 A ATOM 325 C ILE A 112 50.307 17.301 −3.663 1.00 19.03 A ATOM 326 O ILE A 112 49.669 18.350 −3.635 1.00 19.15 A ATOM 327 N LEU A 113 51.622 17.245 −3.472 1.00 20.22 A ATOM 328 CA LEU A 113 52.416 18.442 −3.214 1.00 22.36 A ATOM 329 CB LEU A 113 52.995 18.397 −1.794 1.00 22.13 A ATOM 330 CG LEU A 113 52.042 18.063 −0.646 1.00 22.46 A ATOM 331 CD1 LEU A 113 51.866 16.557 −0.553 1.00 23.81 A ATOM 332 CD2 LEU A 113 52.603 18.595 0.660 1.00 23.68 A ATOM 333 C LEU A 113 53.560 18.547 −4.215 1.00 23.37 A ATOM 334 O LEU A 113 54.300 17.586 −4.424 1.00 23.11 A ATOM 335 N GLU A 114 53.706 19.714 −4.834 1.00 23.88 A ATOM 336 CA GLU A 114 54.771 19.920 −5.806 1.00 26.00 A ATOM 337 CB GLU A 114 54.435 21.111 −6.706 1.00 27.74 A ATOM 338 CG GLU A 114 55.533 21.452 −7.696 1.00 35.07 A ATOM 339 CD GLU A 114 55.220 22.696 −8.497 1.00 39.24 A ATOM 340 OE1 GLU A 114 54.808 23.703 −7.885 1.00 41.45 A ATOM 341 OE2 GLU A 114 55.395 22.670 −9.736 1.00 44.05 A ATOM 342 C GLU A 114 56.087 20.163 −5.067 1.00 24.37 A ATOM 343 O GLU A 114 56.186 21.071 −4.238 1.00 24.43 A ATOM 344 N LYS A 115 57.096 19.350 −5.360 1.00 24.10 A ATOM 345 CA LYS A 115 58.376 19.493 −4.678 1.00 24.93 A ATOM 346 CB LYS A 115 59.339 18.373 −5.103 1.00 23.72 A ATOM 347 CG LYS A 115 59.139 17.080 −4.308 1.00 23.09 A ATOM 348 CD LYS A 115 60.064 15.944 −4.743 1.00 21.92 A ATOM 349 CE LYS A 115 59.691 15.400 −6.117 1.00 22.42 A ATOM 350 NZ LYS A 115 60.447 14.150 −6.448 1.00 19.71 A ATOM 351 C LYS A 115 59.031 20.858 −4.868 1.00 26.87 A ATOM 352 O LYS A 115 59.492 21.469 −3.903 1.00 26.17 A ATOM 353 N ARG A 116 59.058 21.348 −6.102 1.00 28.73 A ATOM 354 CA ARG A 116 59.678 22.638 −6.380 1.00 29.66 A ATOM 355 CB ARG A 116 59.533 22.980 −7.868 1.00 31.29 A ATOM 356 CG ARG A 116 60.047 24.361 −8.267 1.00 33.19 A ATOM 357 CD ARG A 116 61.368 24.710 −7.590 1.00 35.13 A ATOM 358 NE ARG A 116 62.329 23.612 −7.618 1.00 36.42 A ATOM 359 CZ ARG A 116 63.510 23.648 −7.009 1.00 36.18 A ATOM 360 NH1 ARG A 116 63.871 24.729 −6.332 1.00 36.12 A ATOM 361 NH2 ARG A 116 64.324 22.602 −7.067 1.00 35.77 A ATOM 362 C ARG A 116 59.097 23.761 −5.519 1.00 29.70 A ATOM 363 O ARG A 116 59.843 24.515 −4.889 1.00 29.16 A ATOM 364 N HIS A 117 57.773 23.862 −5.472 1.00 27.22 A ATOM 365 CA HIS A 117 57.126 24.903 −4.681 1.00 26.33 A ATOM 366 CB HIS A 117 55.606 24.835 −4.848 1.00 28.41 A ATOM 367 CG HIS A 117 54.881 26.005 −4.258 1.00 31.82 A ATOM 368 CD2 HIS A 117 55.309 27.249 −3.935 1.00 33.19 A ATOM 369 ND1 HIS A 117 53.536 25.974 −3.961 1.00 34.30 A ATOM 370 CE1 HIS A 117 53.165 27.148 −3.480 1.00 34.58 A ATOM 371 NE2 HIS A 117 54.222 27.940 −3.455 1.00 35.18 A ATOM 372 C HIS A 117 57.477 24.780 −3.202 1.00 26.22 A ATOM 373 O HIS A 117 57.737 25.776 −2.534 1.00 25.67 A ATOM 374 N ILE A 118 57.469 23.554 −2.689 1.00 24.94 A ATOM 375 CA ILE A 118 57.792 23.315 −1.285 1.00 23.94 A ATOM 376 CB ILE A 118 57.711 21.812 −0.952 1.00 23.50 A ATOM 377 CG2 ILE A 118 58.374 21.533 0.389 1.00 23.76 A ATOM 378 CG1 ILE A 118 56.246 21.362 −0.959 1.00 24.42 A ATOM 379 CD1 ILE A 118 56.066 19.858 −0.834 1.00 28.06 A ATOM 380 C ILE A 118 59.195 23.821 −0.958 1.00 23.78 A ATOM 381 O ILE A 118 59.402 24.495 0.048 1.00 23.49 A ATOM 382 N ILE A 119 60.153 23.489 −1.815 1.00 23.46 A ATOM 383 CA ILE A 119 61.534 23.913 −1.619 1.00 25.13 A ATOM 384 CB ILE A 119 62.467 23.250 −2.664 1.00 24.25 A ATOM 385 CG2 ILE A 119 63.858 23.890 −2.617 1.00 22.47 A ATOM 386 CG1 ILE A 119 62.540 21.738 −2.395 1.00 25.05 A ATOM 387 CD1 ILE A 119 63.327 20.945 −3.439 1.00 24.62 A ATOM 388 C ILE A 119 61.667 25.435 −1.705 1.00 25.96 A ATOM 389 O ILE A 119 62.330 26.051 −0.872 1.00 24.78 A ATOM 390 N LYS A 120 61.028 26.039 −2.704 1.00 27.67 A ATOM 391 CA LYS A 120 61.100 27.489 −2.879 1.00 30.29 A ATOM 392 CB LYS A 120 60.242 27.940 −4.060 1.00 32.34 A ATOM 393 CG LYS A 120 60.674 27.407 −5.409 1.00 39.30 A ATOM 394 CD LYS A 120 59.765 27.950 −6.512 1.00 45.19 A ATOM 395 CE LYS A 120 58.294 27.636 −6.218 1.00 46.48 A ATOM 396 NZ LYS A 120 57.363 28.155 −7.252 1.00 46.49 A ATOM 397 C LYS A 120 60.647 28.247 −1.638 1.00 30.89 A ATOM 398 O LYS A 120 61.303 29.198 −1.217 1.00 32.48 A ATOM 399 N GLU A 121 59.527 27.825 −1.055 1.00 29.82 A ATOM 400 CA GLU A 121 58.986 28.488 0.128 1.00 30.33 A ATOM 401 CB GLU A 121 57.455 28.416 0.117 1.00 33.04 A ATOM 402 CG GLU A 121 56.794 29.021 −1.120 1.00 36.45 A ATOM 403 CD GLU A 121 57.221 30.456 −1.373 1.00 39.88 A ATOM 404 OE1 GLU A 121 57.200 31.264 −0.420 1.00 40.53 A ATOM 405 OE2 GLU A 121 57.573 30.778 −2.529 1.00 43.24 A ATOM 406 C GLU A 121 59.511 27.930 1.451 1.00 30.37 A ATOM 407 O GLU A 121 58.946 28.204 2.513 1.00 31.24 A ATOM 408 N ASN A 122 60.588 27.151 1.390 1.00 29.03 A ATOM 409 CA ASN A 122 61.183 26.573 2.594 1.00 28.46 A ATOM 410 CB ASN A 122 61.836 27.673 3.436 1.00 31.28 A ATOM 411 CG ASN A 122 62.945 28.395 2.698 1.00 34.12 A ATOM 412 OD1 ASN A 122 62.697 29.143 1.754 1.00 35.57 A ATOM 413 ND2 ASN A 122 64.181 28.169 3.127 1.00 35.73 A ATOM 414 C ASN A 122 60.157 25.835 3.456 1.00 26.89 A ATOM 415 O ASN A 122 60.085 26.055 4.663 1.00 27.23 A ATOM 416 N LYS A 123 59.375 24.955 2.842 1.00 23.99 A ATOM 417 CA LYS A 123 58.358 24.210 3.574 1.00 22.43 A ATOM 418 CB LYS A 123 57.031 24.248 2.810 1.00 21.97 A ATOM 419 CG LYS A 123 56.475 25.645 2.599 1.00 25.68 A ATOM 420 CD LYS A 123 56.253 26.354 3.927 1.00 27.54 A ATOM 421 CE LYS A 123 55.822 27.796 3.716 1.00 31.30 A ATOM 422 NZ LYS A 123 55.756 28.540 5.004 1.00 33.21 A ATOM 423 C LYS A 123 58.748 22.759 3.821 1.00 22.20 A ATOM 424 O LYS A 123 57.924 21.960 4.264 1.00 22.50 A ATOM 425 N VAL A 124 59.997 22.412 3.535 1.00 20.59 A ATOM 426 CA VAL A 124 60.439 21.039 3.730 1.00 20.25 A ATOM 427 CB VAL A 124 61.922 20.850 3.328 1.00 19.43 A ATOM 428 CG1 VAL A 124 62.346 19.407 3.573 1.00 18.69 A ATOM 429 CG2 VAL A 124 62.104 21.195 1.853 1.00 18.21 A ATOM 430 C VAL A 124 60.236 20.561 5.163 1.00 19.53 A ATOM 431 O VAL A 124 59.841 19.418 5.385 1.00 20.02 A ATOM 432 N PRO A 125 60.513 21.422 6.159 1.00 20.01 A ATOM 433 CD PRO A 125 61.178 22.738 6.118 1.00 18.69 A ATOM 434 CA PRO A 125 60.318 20.979 7.544 1.00 19.88 A ATOM 435 CB PRO A 125 60.793 22.180 8.363 1.00 19.95 A ATOM 436 CG PRO A 125 61.839 22.805 7.479 1.00 18.85 A ATOM 437 C PRO A 125 58.848 20.642 7.824 1.00 19.76 A ATOM 438 O PRO A 125 58.544 19.700 8.550 1.00 16.99 A ATOM 439 N TYR A 126 57.947 21.418 7.235 1.00 18.98 A ATOM 440 CA TYR A 126 56.516 21.220 7.435 1.00 21.97 A ATOM 441 CB TYR A 126 55.752 22.448 6.933 1.00 25.17 A ATOM 442 CG TYR A 126 56.040 23.690 7.748 1.00 30.98 A ATOM 443 CD1 TYR A 126 55.438 23.886 8.991 1.00 33.95 A ATOM 444 CE1 TYR A 126 55.721 25.015 9.763 1.00 36.60 A ATOM 445 CD2 TYR A 126 56.938 24.657 7.292 1.00 35.43 A ATOM 446 CE2 TYR A 126 57.231 25.792 8.058 1.00 37.20 A ATOM 447 CZ TYR A 126 56.618 25.962 9.291 1.00 37.40 A ATOM 448 OH TYR A 126 56.903 27.073 10.052 1.00 40.85 A ATOM 449 C TYR A 126 55.990 19.956 6.762 1.00 21.35 A ATOM 450 O TYR A 126 55.265 19.175 7.383 1.00 20.49 A ATOM 451 N VAL A 127 56.354 19.746 5.501 1.00 18.16 A ATOM 452 CA VAL A 127 55.892 18.562 4.790 1.00 17.58 A ATOM 453 CB VAL A 127 56.308 18.596 3.308 1.00 17.45 A ATOM 454 CG1 VAL A 127 55.786 17.350 2.600 1.00 17.97 A ATOM 455 CG2 VAL A 127 55.751 19.850 2.641 1.00 14.90 A ATOM 456 C VAL A 127 56.459 17.306 5.448 1.00 18.39 A ATOM 457 O VAL A 127 55.769 16.298 5.583 1.00 18.14 A ATOM 458 N THR A 128 57.716 17.381 5.869 1.00 17.50 A ATOM 459 CA THR A 128 58.375 16.260 6.530 1.00 18.54 A ATOM 460 CB THR A 128 59.861 16.586 6.805 1.00 18.01 A ATOM 461 OG1 THR A 128 60.537 16.804 5.559 1.00 21.14 A ATOM 462 CG2 THR A 128 60.536 15.446 7.545 1.00 17.95 A ATOM 463 C THR A 128 57.676 15.941 7.856 1.00 19.49 A ATOM 464 O THR A 128 57.438 14.776 8.179 1.00 18.76 A ATOM 465 N ARG A 129 57.345 16.981 8.619 1.00 19.60 A ATOM 466 CA ARG A 129 56.673 16.804 9.904 1.00 20.12 A ATOM 467 CB ARG A 129 56.534 18.144 10.621 1.00 21.33 A ATOM 468 CG ARG A 129 55.948 18.029 12.023 1.00 28.02 A ATOM 469 CD ARG A 129 55.721 19.404 12.597 1.00 31.25 A ATOM 470 NE ARG A 129 56.940 20.205 12.560 1.00 37.78 A ATOM 471 CZ ARG A 129 56.962 21.524 12.391 1.00 40.10 A ATOM 472 NH1 ARG A 129 55.828 22.197 12.239 1.00 40.03 A ATOM 473 NH2 ARG A 129 58.119 22.170 12.374 1.00 44.58 A ATOM 474 C ARG A 129 55.288 16.186 9.729 1.00 20.08 A ATOM 475 O ARG A 129 54.891 15.305 10.496 1.00 20.40 A ATOM 476 N GLU A 130 54.553 16.654 8.724 1.00 18.79 A ATOM 477 CA GLU A 130 53.222 16.125 8.454 1.00 20.10 A ATOM 478 CB GLU A 130 52.638 16.749 7.183 1.00 19.92 A ATOM 479 CG GLU A 130 51.350 16.087 6.708 1.00 27.85 A ATOM 480 CD GLU A 130 50.581 16.933 5.707 1.00 29.72 A ATOM 481 OE1 GLU A 130 51.216 17.528 4.814 1.00 33.46 A ATOM 482 OE2 GLU A 130 49.339 16.996 5.807 1.00 30.74 A ATOM 483 C GLU A 130 53.301 14.615 8.295 1.00 19.81 A ATOM 484 O GLU A 130 52.553 13.875 8.935 1.00 18.37 A ATOM 485 N ARG A 131 54.219 14.162 7.447 1.00 20.41 A ATOM 486 CA ARG A 131 54.397 12.735 7.202 1.00 22.45 A ATOM 487 CB ARG A 131 55.442 12.511 6.098 1.00 25.16 A ATOM 488 CG ARG A 131 55.742 11.043 5.840 1.00 28.75 A ATOM 489 CD ARG A 131 56.736 10.837 4.708 1.00 33.75 A ATOM 490 NE ARG A 131 57.020 9.415 4.520 1.00 40.07 A ATOM 491 CZ ARG A 131 57.756 8.915 3.532 1.00 43.07 A ATOM 492 NH1 ARG A 131 58.293 9.721 2.625 1.00 44.91 A ATOM 493 NH2 ARG A 131 57.955 7.606 3.449 1.00 44.45 A ATOM 494 C ARG A 131 54.820 11.982 8.466 1.00 23.24 A ATOM 495 O ARG A 131 54.241 10.948 8.804 1.00 23.86 A ATOM 496 N ASP A 132 55.831 12.497 9.160 1.00 21.99 A ATOM 497 CA ASP A 132 56.318 11.850 10.370 1.00 22.04 A ATOM 498 CB ASP A 132 57.570 12.564 10.888 1.00 23.72 A ATOM 499 CG ASP A 132 58.750 12.442 9.932 1.00 27.77 A ATOM 500 OD1 ASP A 132 58.681 11.620 8.989 1.00 27.34 A ATOM 501 OD2 ASP A 132 59.753 13.163 10.128 1.00 28.70 A ATOM 502 C ASP A 132 55.258 11.772 11.474 1.00 21.69 A ATOM 503 O ASP A 132 55.077 10.723 12.092 1.00 22.75 A ATOM 504 N VAL A 133 54.551 12.868 11.725 1.00 19.54 A ATOM 505 CA VAL A 133 53.525 12.843 12.759 1.00 18.52 A ATOM 506 CB VAL A 133 52.908 14.244 12.990 1.00 19.26 A ATOM 507 CG1 VAL A 133 51.708 14.135 13.918 1.00 18.79 A ATOM 508 CG2 VAL A 133 53.953 15.180 13.604 1.00 18.80 A ATOM 509 C VAL A 133 52.419 11.854 12.398 1.00 19.46 A ATOM 510 O VAL A 133 52.073 10.991 13.200 1.00 19.94 A ATOM 511 N MET A 134 51.878 11.957 11.187 1.00 19.15 A ATOM 512 CA MET A 134 50.807 11.052 10.792 1.00 21.25 A ATOM 513 CB MET A 134 50.309 11.381 9.383 1.00 17.34 A ATOM 514 CG MET A 134 49.615 12.730 9.302 1.00 20.00 A ATOM 515 SD MET A 134 48.643 12.952 7.798 1.00 24.21 A ATOM 516 CE MET A 134 47.033 12.434 8.400 1.00 23.20 A ATOM 517 C MET A 134 51.203 9.582 10.881 1.00 22.43 A ATOM 518 O MET A 134 50.384 8.741 11.249 1.00 23.82 A ATOM 519 N SER A 135 52.454 9.273 10.556 1.00 23.09 A ATOM 520 CA SER A 135 52.939 7.895 10.615 1.00 26.13 A ATOM 521 CB SER A 135 54.356 7.798 10.039 1.00 26.17 A ATOM 522 OG SER A 135 54.383 8.177 8.673 1.00 31.91 A ATOM 523 C SER A 135 52.957 7.358 12.045 1.00 26.58 A ATOM 524 O SER A 135 52.926 6.148 12.261 1.00 26.42 A ATOM 525 N ARG A 136 53.014 8.261 13.018 1.00 25.65 A ATOM 526 CA ARG A 136 53.056 7.870 14.425 1.00 27.47 A ATOM 527 CB ARG A 136 53.823 8.914 15.238 1.00 27.97 A ATOM 528 CG ARG A 136 55.283 9.082 14.857 1.00 32.00 A ATOM 529 CD ARG A 136 55.904 10.218 15.664 1.00 33.03 A ATOM 530 NE ARG A 136 55.602 10.073 17.084 1.00 36.11 A ATOM 531 CZ ARG A 136 55.867 10.990 18.007 1.00 39.74 A ATOM 532 NH1 ARG A 136 56.449 12.132 17.661 1.00 40.55 A ATOM 533 NH2 ARG A 136 55.540 10.769 19.276 1.00 36.72 A ATOM 534 C ARG A 136 51.667 7.709 15.036 1.00 26.38 A ATOM 535 O ARG A 136 51.516 7.121 16.106 1.00 27.06 A ATOM 536 N LEU A 137 50.655 8.235 14.360 1.00 24.77 A ATOM 537 CA LEU A 137 49.294 8.162 14.870 1.00 24.70 A ATOM 538 CB LEU A 137 48.483 9.363 14.371 1.00 24.52 A ATOM 539 CG LEU A 137 49.050 10.760 14.662 1.00 26.67 A ATOM 540 CD1 LEU A 137 48.075 11.813 14.141 1.00 27.25 A ATOM 541 CD2 LEU A 137 49.279 10.945 16.155 1.00 27.09 A ATOM 542 C LEU A 137 48.592 6.868 14.473 1.00 25.20 A ATOM 543 O LEU A 137 48.619 6.469 13.309 1.00 25.99 A ATOM 544 N ASP A 138 47.971 6.218 15.451 1.00 21.89 A ATOM 545 CA ASP A 138 47.239 4.977 15.219 1.00 21.35 A ATOM 546 CB ASP A 138 48.124 3.761 15.523 1.00 22.14 A ATOM 547 CG ASP A 138 47.432 2.448 15.201 1.00 24.90 A ATOM 548 OD1 ASP A 138 46.631 2.423 14.241 1.00 24.78 A ATOM 549 OD2 ASP A 138 47.691 1.443 15.897 1.00 25.39 A ATOM 550 C ASP A 138 46.031 4.991 16.138 1.00 20.47 A ATOM 551 O ASP A 138 45.967 4.248 17.118 1.00 19.06 A ATOM 552 N HIS A 139 45.075 5.852 15.810 1.00 18.27 A ATOM 553 CA HIS A 139 43.869 6.016 16.606 1.00 18.21 A ATOM 554 CB HIS A 139 44.096 7.157 17.612 1.00 15.84 A ATOM 555 CG HIS A 139 42.985 7.332 18.600 1.00 15.24 A ATOM 556 CD2 HIS A 139 42.884 6.964 19.900 1.00 13.97 A ATOM 557 ND1 HIS A 139 41.791 7.943 18.280 1.00 14.74 A ATOM 558 CE1 HIS A 139 41.002 7.944 19.341 1.00 14.19 A ATOM 559 NE2 HIS A 139 41.641 7.356 20.336 1.00 14.15 A ATOM 560 C HIS A 139 42.715 6.330 15.654 1.00 18.50 A ATOM 561 O HIS A 139 42.879 7.080 14.693 1.00 20.80 A ATOM 562 N PRO A 140 41.527 5.767 15.913 1.00 18.32 A ATOM 563 CD PRO A 140 41.143 4.984 17.100 1.00 16.71 A ATOM 564 CA PRO A 140 40.367 6.001 15.048 1.00 17.43 A ATOM 565 CB PRO A 140 39.273 5.157 15.704 1.00 16.64 A ATOM 566 CG PRO A 140 39.643 5.204 17.152 1.00 18.43 A ATOM 567 C PRO A 140 39.914 7.441 14.803 1.00 18.77 A ATOM 568 O PRO A 140 39.207 7.695 13.831 1.00 19.88 A ATOM 569 N PHE A 141 40.301 8.381 15.664 1.00 17.14 A ATOM 570 CA PHE A 141 39.874 9.767 15.477 1.00 16.42 A ATOM 571 CB PHE A 141 39.568 10.422 16.836 1.00 14.60 A ATOM 572 CG PHE A 141 38.386 9.817 17.556 1.00 15.26 A ATOM 573 CD1 PHE A 141 37.335 9.234 16.842 1.00 14.78 A ATOM 574 CD2 PHE A 141 38.297 9.880 18.942 1.00 13.70 A ATOM 575 CE1 PHE A 141 36.215 8.727 17.502 1.00 16.94 A ATOM 576 CE2 PHE A 141 37.178 9.375 19.615 1.00 15.75 A ATOM 577 CZ PHE A 141 36.135 8.799 18.893 1.00 16.89 A ATOM 578 C PHE A 141 40.857 10.641 14.694 1.00 16.15 A ATOM 579 O PHE A 141 40.799 11.871 14.761 1.00 17.35 A ATOM 580 N PHE A 142 41.748 10.011 13.941 1.00 15.88 A ATOM 581 CA PHE A 142 42.727 10.756 13.154 1.00 17.89 A ATOM 582 CB PHE A 142 44.115 10.645 13.793 1.00 17.57 A ATOM 583 CG PHE A 142 44.240 11.371 15.103 1.00 18.74 A ATOM 584 CD1 PHE A 142 44.559 12.726 15.135 1.00 17.77 A ATOM 585 CD2 PHE A 142 43.997 10.711 16.304 1.00 18.74 A ATOM 586 CE1 PHE A 142 44.632 13.417 16.347 1.00 15.77 A ATOM 587 CE2 PHE A 142 44.065 11.393 17.522 1.00 17.56 A ATOM 588 CZ PHE A 142 44.383 12.747 17.542 1.00 17.14 A ATOM 589 C PHE A 142 42.793 10.231 11.729 1.00 19.12 A ATOM 590 O PHE A 142 42.659 9.030 11.504 1.00 20.01 A ATOM 591 N VAL A 143 42.978 11.135 10.769 1.00 18.72 A ATOM 592 CA VAL A 143 43.102 10.735 9.371 1.00 18.52 A ATOM 593 CB VAL A 143 43.294 11.961 8.440 1.00 20.66 A ATOM 594 CG1 VAL A 143 43.843 11.521 7.080 1.00 21.29 A ATOM 595 CG2 VAL A 143 41.958 12.673 8.252 1.00 22.97 A ATOM 596 C VAL A 143 44.342 9.865 9.330 1.00 18.68 A ATOM 597 O VAL A 143 45.355 10.199 9.943 1.00 18.42 A ATOM 598 N LYS A 144 44.259 8.745 8.623 1.00 18.30 A ATOM 599 CA LYS A 144 45.384 7.824 8.535 1.00 18.78 A ATOM 600 CB LYS A 144 44.889 6.373 8.608 1.00 22.27 A ATOM 601 CG LYS A 144 46.017 5.340 8.557 1.00 29.72 A ATOM 602 CD LYS A 144 45.491 3.912 8.674 1.00 34.16 A ATOM 603 CE LYS A 144 46.631 2.896 8.577 1.00 37.67 A ATOM 604 NZ LYS A 144 46.138 1.484 8.629 1.00 39.02 A ATOM 605 C LYS A 144 46.192 8.002 7.261 1.00 18.53 A ATOM 606 O LYS A 144 45.643 8.314 6.200 1.00 18.18 A ATOM 607 N LEU A 145 47.502 7.816 7.385 1.00 16.79 A ATOM 608 CA LEU A 145 48.411 7.900 6.251 1.00 17.45 A ATOM 609 CB LEU A 145 49.686 8.653 6.641 1.00 18.82 A ATOM 610 CG LEU A 145 50.734 8.902 5.549 1.00 20.23 A ATOM 611 CD1 LEU A 145 51.836 9.799 6.093 1.00 18.83 A ATOM 612 CD2 LEU A 145 51.317 7.581 5.069 1.00 19.79 A ATOM 613 C LEU A 145 48.739 6.450 5.907 1.00 19.19 A ATOM 614 O LEU A 145 49.451 5.772 6.659 1.00 17.36 A ATOM 615 N TYR A 146 48.215 5.972 4.782 1.00 17.28 A ATOM 616 CA TYR A 146 48.444 4.593 4.358 1.00 17.57 A ATOM 617 CB TYR A 146 47.288 4.098 3.486 1.00 17.74 A ATOM 618 CG TYR A 146 45.981 3.926 4.214 1.00 17.50 A ATOM 619 CD1 TYR A 146 45.099 4.995 4.377 1.00 16.50 A ATOM 620 CE1 TYR A 146 43.881 4.827 5.039 1.00 17.10 A ATOM 621 CD2 TYR A 146 45.620 2.686 4.735 1.00 18.28 A ATOM 622 CE2 TYR A 146 44.411 2.506 5.399 1.00 19.84 A ATOM 623 CZ TYR A 146 43.547 3.576 5.544 1.00 17.53 A ATOM 624 OH TYR A 146 42.342 3.376 6.169 1.00 20.67 A ATOM 625 C TYR A 146 49.735 4.376 3.582 1.00 18.72 A ATOM 626 O TYR A 146 50.382 3.338 3.715 1.00 19.51 A ATOM 627 N PHE A 147 50.110 5.350 2.765 1.00 18.09 A ATOM 628 CA PHE A 147 51.307 5.203 1.952 1.00 17.20 A ATOM 629 CB PHE A 147 51.007 4.258 0.783 1.00 16.77 A ATOM 630 CG PHE A 147 49.835 4.699 −0.070 1.00 17.75 A ATOM 631 CD1 PHE A 147 49.967 5.752 −0.975 1.00 16.58 A ATOM 632 CD2 PHE A 147 48.595 4.075 0.053 1.00 18.07 A ATOM 633 CE1 PHE A 147 48.886 6.178 −1.742 1.00 19.62 A ATOM 634 CE2 PHE A 147 47.503 4.492 −0.710 1.00 18.56 A ATOM 635 CZ PHE A 147 47.647 5.546 −1.610 1.00 19.27 A ATOM 636 C PHE A 147 51.768 6.533 1.395 1.00 17.13 A ATOM 637 O PHE A 147 51.045 7.528 1.452 1.00 14.43 A ATOM 638 N THR A 148 52.981 6.534 0.854 1.00 17.12 A ATOM 639 CA THR A 148 53.541 7.718 0.232 1.00 17.96 A ATOM 640 CB THR A 148 54.449 8.531 1.197 1.00 21.51 A ATOM 641 OG1 THR A 148 55.605 7.760 1.537 1.00 18.83 A ATOM 642 CG2 THR A 148 53.700 8.897 2.472 1.00 19.60 A ATOM 643 C THR A 148 54.386 7.262 −0.946 1.00 20.31 A ATOM 644 O THR A 148 54.860 6.124 −0.991 1.00 18.94 A ATOM 645 N PHE A 149 54.543 8.149 −1.916 1.00 19.16 A ATOM 646 CA PHE A 149 55.368 7.877 −3.073 1.00 18.01 A ATOM 647 CB PHE A 149 54.748 6.801 −3.989 1.00 17.23 A ATOM 648 CG PHE A 149 53.389 7.144 −4.544 1.00 16.88 A ATOM 649 CD1 PHE A 149 53.262 7.888 −5.712 1.00 18.58 A ATOM 650 CD2 PHE A 149 52.235 6.668 −3.927 1.00 17.31 A ATOM 651 CE1 PHE A 149 52.007 8.149 −6.267 1.00 19.26 A ATOM 652 CE2 PHE A 149 50.972 6.923 −4.470 1.00 19.17 A ATOM 653 CZ PHE A 149 50.858 7.663 −5.642 1.00 19.60 A ATOM 654 C PHE A 149 55.542 9.205 −3.774 1.00 20.85 A ATOM 655 O PHE A 149 54.934 10.200 −3.376 1.00 19.76 A ATOM 656 N GLN A 150 56.398 9.241 −4.782 1.00 19.79 A ATOM 657 CA GLN A 150 56.636 10.481 −5.497 1.00 24.03 A ATOM 658 CB GLN A 150 57.659 11.347 −4.739 1.00 24.45 A ATOM 659 CG GLN A 150 58.986 10.645 −4.414 1.00 26.28 A ATOM 660 CD GLN A 150 59.988 11.558 −3.692 1.00 29.02 A ATOM 661 OE1 GLN A 150 60.693 12.353 −4.321 1.00 27.05 A ATOM 662 NE2 GLN A 150 60.042 11.449 −2.365 1.00 26.47 A ATOM 663 C GLN A 150 57.160 10.203 −6.885 1.00 23.88 A ATOM 664 O GLN A 150 57.673 9.118 −7.158 1.00 24.79 A ATOM 665 N ASP A 151 56.987 11.171 −7.774 1.00 25.88 A ATOM 666 CA ASP A 151 57.527 11.047 −9.117 1.00 26.49 A ATOM 667 CB ASP A 151 56.437 11.126 −10.199 1.00 24.54 A ATOM 668 CG ASP A 151 55.544 12.336 −10.064 1.00 24.95 A ATOM 669 OD1 ASP A 151 56.005 13.379 −9.561 1.00 22.44 A ATOM 670 OD2 ASP A 151 54.369 12.242 −10.490 1.00 25.72 A ATOM 671 C ASP A 151 58.515 12.203 −9.220 1.00 28.63 A ATOM 672 O ASP A 151 58.890 12.780 −8.194 1.00 27.83 A ATOM 673 N ASP A 152 58.934 12.560 −10.426 1.00 29.21 A ATOM 674 CA ASP A 152 59.907 13.636 −10.562 1.00 31.88 A ATOM 675 CB ASP A 152 60.325 13.792 −12.026 1.00 33.94 A ATOM 676 CG ASP A 152 61.033 12.564 −12.557 1.00 38.88 A ATOM 677 OD1 ASP A 152 61.817 11.959 −11.791 1.00 39.67 A ATOM 678 OD2 ASP A 152 60.817 12.211 −13.738 1.00 41.57 A ATOM 679 C ASP A 152 59.487 14.994 −10.013 1.00 30.90 A ATOM 680 O ASP A 152 60.316 15.735 −9.482 1.00 31.69 A ATOM 681 N GLU A 153 58.207 15.322 −10.107 1.00 29.44 A ATOM 682 CA GLU A 153 57.767 16.632 −9.646 1.00 28.69 A ATOM 683 CB GLU A 153 56.984 17.327 −10.766 1.00 32.90 A ATOM 684 CG GLU A 153 57.451 16.987 −12.183 1.00 40.57 A ATOM 685 CD GLU A 153 56.920 15.643 −12.675 1.00 45.78 A ATOM 686 OE1 GLU A 153 55.682 15.482 −12.760 1.00 48.91 A ATOM 687 OE2 GLU A 153 57.736 14.747 −12.979 1.00 48.95 A ATOM 688 C GLU A 153 56.929 16.683 −8.372 1.00 26.43 A ATOM 689 O GLU A 153 56.947 17.688 −7.660 1.00 25.08 A ATOM 690 N LYS A 154 56.205 15.610 −8.069 1.00 22.39 A ATOM 691 CA LYS A 154 55.318 15.631 −6.912 1.00 21.43 A ATOM 692 CB LYS A 154 53.861 15.628 −7.398 1.00 20.33 A ATOM 693 CG LYS A 154 53.505 16.716 −8.403 1.00 21.92 A ATOM 694 CD LYS A 154 52.211 16.375 −9.146 1.00 19.70 A ATOM 695 CE LYS A 154 51.775 17.503 −10.077 1.00 20.04 A ATOM 696 NZ LYS A 154 50.631 17.094 −10.951 1.00 19.97 A ATOM 697 C LYS A 154 55.458 14.522 −5.881 1.00 20.43 A ATOM 698 O LYS A 154 55.949 13.426 −6.173 1.00 21.13 A ATOM 699 N LEU A 155 54.985 14.832 −4.676 1.00 19.69 A ATOM 700 CA LEU A 155 54.950 13.900 −3.553 1.00 19.10 A ATOM 701 CB LEU A 155 55.362 14.588 −2.252 1.00 19.65 A ATOM 702 CG LEU A 155 56.740 15.234 −2.129 1.00 21.20 A ATOM 703 CD1 LEU A 155 56.848 15.918 −0.770 1.00 23.42 A ATOM 704 CD2 LEU A 155 57.816 14.174 −2.277 1.00 23.08 A ATOM 705 C LEU A 155 53.478 13.507 −3.427 1.00 18.87 A ATOM 706 O LEU A 155 52.600 14.348 −3.620 1.00 18.61 A ATOM 707 N TYR A 156 53.209 12.249 −3.091 1.00 15.02 A ATOM 708 CA TYR A 156 51.834 11.783 −2.934 1.00 16.29 A ATOM 709 CB TYR A 156 51.470 10.769 −4.029 1.00 14.20 A ATOM 710 CG TYR A 156 51.603 11.273 −5.449 1.00 17.29 A ATOM 711 CD1 TYR A 156 52.857 11.429 −6.045 1.00 16.46 A ATOM 712 CE1 TYR A 156 52.978 11.884 −7.360 1.00 18.68 A ATOM 713 CD2 TYR A 156 50.474 11.588 −6.202 1.00 16.43 A ATOM 714 CE2 TYR A 156 50.583 12.048 −7.512 1.00 16.31 A ATOM 715 CZ TYR A 156 51.835 12.192 −8.083 1.00 18.17 A ATOM 716 OH TYR A 156 51.941 12.651 −9.371 1.00 17.47 A ATOM 717 C TYR A 156 51.657 11.108 −1.572 1.00 16.32 A ATOM 718 O TYR A 156 52.412 10.197 −1.235 1.00 16.27 A ATOM 719 N PHE A 157 50.678 11.568 −0.792 1.00 15.47 A ATOM 720 CA PHE A 157 50.385 10.966 0.508 1.00 16.66 A ATOM 721 CB PHE A 157 50.324 12.014 1.629 1.00 16.91 A ATOM 722 CG PHE A 157 51.631 12.708 1.907 1.00 18.96 A ATOM 723 CD1 PHE A 157 52.821 12.261 1.340 1.00 20.31 A ATOM 724 CD2 PHE A 157 51.664 13.829 2.732 1.00 21.12 A ATOM 725 CE1 PHE A 157 54.025 12.926 1.585 1.00 22.08 A ATOM 726 CE2 PHE A 157 52.865 14.500 2.982 1.00 22.18 A ATOM 727 CZ PHE A 157 54.045 14.045 2.405 1.00 21.27 A ATOM 728 C PHE A 157 49.016 10.308 0.404 1.00 16.52 A ATOM 729 O PHE A 157 48.029 10.979 0.110 1.00 17.32 A ATOM 730 N GLY A 158 48.953 9.002 0.644 1.00 15.97 A ATOM 731 CA GLY A 158 47.684 8.299 0.572 1.00 16.13 A ATOM 732 C GLY A 158 47.000 8.383 1.920 1.00 14.94 A ATOM 733 O GLY A 158 47.445 7.756 2.879 1.00 16.28 A ATOM 734 N LEU A 159 45.915 9.145 1.989 1.00 13.50 A ATOM 735 CA LEU A 159 45.191 9.340 3.241 1.00 15.20 A ATOM 736 CB LEU A 159 45.031 10.835 3.517 1.00 14.20 A ATOM 737 CG LEU A 159 46.270 11.726 3.385 1.00 19.00 A ATOM 738 CD1 LEU A 159 45.847 13.188 3.477 1.00 17.12 A ATOM 739 CD2 LEU A 159 47.275 11.390 4.471 1.00 14.71 A ATOM 740 C LEU A 159 43.809 8.716 3.232 1.00 15.53 A ATOM 741 O LEU A 159 43.232 8.472 2.177 1.00 16.05 A ATOM 742 N SER A 160 43.268 8.469 4.418 1.00 15.86 A ATOM 743 CA SER A 160 41.932 7.917 4.498 1.00 19.01 A ATOM 744 CB SER A 160 41.566 7.582 5.949 1.00 22.90 A ATOM 745 OG SER A 160 41.901 8.629 6.833 1.00 24.18 A ATOM 746 C SER A 160 40.987 8.968 3.924 1.00 20.43 A ATOM 747 O SER A 160 41.213 10.173 4.062 1.00 19.96 A ATOM 748 N TYR A 161 39.945 8.508 3.250 1.00 19.20 A ATOM 749 CA TYR A 161 38.975 9.406 2.644 1.00 20.37 A ATOM 750 CB TYR A 161 38.471 8.785 1.332 1.00 20.00 A ATOM 751 CG TYR A 161 37.314 9.502 0.666 1.00 20.72 A ATOM 752 CD1 TYR A 161 37.222 10.895 0.682 1.00 18.22 A ATOM 753 CE1 TYR A 161 36.180 11.557 0.029 1.00 22.24 A ATOM 754 CD2 TYR A 161 36.333 8.784 −0.020 1.00 20.53 A ATOM 755 CE2 TYR A 161 35.287 9.436 −0.678 1.00 24.24 A ATOM 756 CZ TYR A 161 35.218 10.822 −0.648 1.00 22.32 A ATOM 757 OH TYR A 161 34.194 11.471 −1.298 1.00 23.03 A ATOM 758 C TYR A 161 37.812 9.681 3.598 1.00 20.14 A ATOM 759 O TYR A 161 36.959 8.819 3.810 1.00 19.53 A ATOM 760 N ALA A 162 37.791 10.880 4.178 1.00 19.92 A ATOM 761 CA ALA A 162 36.721 11.271 5.099 1.00 21.07 A ATOM 762 CB ALA A 162 37.187 12.419 6.002 1.00 19.60 A ATOM 763 C ALA A 162 35.542 11.712 4.238 1.00 22.07 A ATOM 764 O ALA A 162 35.436 12.875 3.860 1.00 20.66 A ATOM 765 N LYS A 163 34.653 10.769 3.945 1.00 23.27 A ATOM 766 CA LYS A 163 33.503 11.017 3.080 1.00 27.12 A ATOM 767 CB LYS A 163 32.663 9.741 2.963 1.00 29.68 A ATOM 768 CG LYS A 163 33.455 8.524 2.515 1.00 37.67 A ATOM 769 CD LYS A 163 32.556 7.310 2.321 1.00 42.24 A ATOM 770 CE LYS A 163 33.373 6.034 2.185 1.00 44.48 A ATOM 771 NZ LYS A 163 34.143 5.735 3.430 1.00 44.88 A ATOM 772 C LYS A 163 32.581 12.186 3.411 1.00 25.78 A ATOM 773 O LYS A 163 32.103 12.863 2.506 1.00 26.53 A ATOM 774 N ASN A 164 32.327 12.441 4.689 1.00 24.57 A ATOM 775 CA ASN A 164 31.420 13.522 5.033 1.00 23.77 A ATOM 776 CB ASN A 164 30.610 13.129 6.265 1.00 25.02 A ATOM 777 CG ASN A 164 29.537 12.101 5.932 1.00 27.54 A ATOM 778 OD1 ASN A 164 28.772 12.281 4.983 1.00 28.79 A ATOM 779 ND2 ASN A 164 29.475 11.024 6.704 1.00 27.13 A ATOM 780 C ASN A 164 31.999 14.931 5.169 1.00 24.43 A ATOM 781 O ASN A 164 31.306 15.856 5.589 1.00 23.98 A ATOM 782 N GLY A 165 33.262 15.097 4.795 1.00 21.56 A ATOM 783 CA GLY A 165 33.873 16.414 4.836 1.00 24.39 A ATOM 784 C GLY A 165 34.191 17.043 6.181 1.00 23.62 A ATOM 785 O GLY A 165 34.380 16.352 7.177 1.00 23.26 A ATOM 786 N GLU A 166 34.234 18.373 6.186 1.00 23.22 A ATOM 787 CA GLU A 166 34.563 19.176 7.362 1.00 24.54 A ATOM 788 CB GLU A 166 35.055 20.558 6.913 1.00 25.04 A ATOM 789 CG GLU A 166 36.419 20.569 6.229 1.00 26.48 A ATOM 790 CD GLU A 166 36.699 21.889 5.517 1.00 30.02 A ATOM 791 OE1 GLU A 166 36.081 22.906 5.889 1.00 29.33 A ATOM 792 OE2 GLU A 166 37.544 21.916 4.596 1.00 30.48 A ATOM 793 C GLU A 166 33.436 19.372 8.369 1.00 24.44 A ATOM 794 O GLU A 166 32.279 19.541 8.001 1.00 22.76 A ATOM 795 N LEU A 167 33.791 19.370 9.649 1.00 22.95 A ATOM 796 CA LEU A 167 32.813 19.581 10.707 1.00 22.26 A ATOM 797 CB LEU A 167 33.497 19.481 12.073 1.00 22.32 A ATOM 798 CG LEU A 167 32.706 19.923 13.306 1.00 22.04 A ATOM 799 CD1 LEU A 167 31.454 19.074 13.463 1.00 19.66 A ATOM 800 CD2 LEU A 167 33.597 19.805 14.537 1.00 21.17 A ATOM 801 C LEU A 167 32.193 20.971 10.529 1.00 23.49 A ATOM 802 O LEU A 167 31.047 21.209 10.907 1.00 23.56 A ATOM 803 N LEU A 168 32.960 21.887 9.948 1.00 24.25 A ATOM 804 CA LEU A 168 32.473 23.245 9.722 1.00 26.64 A ATOM 805 CB LEU A 168 33.560 24.099 9.066 1.00 25.62 A ATOM 806 CG LEU A 168 33.198 25.546 8.707 1.00 27.34 A ATOM 807 CD1 LEU A 168 32.718 26.296 9.946 1.00 26.42 A ATOM 808 CD2 LEU A 168 34.418 26.238 8.119 1.00 26.74 A ATOM 809 C LEU A 168 31.234 23.218 8.829 1.00 27.13 A ATOM 810 O LEU A 168 30.297 23.989 9.030 1.00 26.01 A ATOM 811 N LYS A 169 31.233 22.320 7.848 1.00 26.41 A ATOM 812 CA LYS A 169 30.106 22.210 6.934 1.00 27.70 A ATOM 813 CB LYS A 169 30.324 21.064 5.945 1.00 30.49 A ATOM 814 CG LYS A 169 29.151 20.854 4.993 1.00 32.47 A ATOM 815 CD LYS A 169 29.407 19.728 3.998 1.00 35.98 A ATOM 816 CE LYS A 169 29.462 18.372 4.683 1.00 38.53 A ATOM 817 NZ LYS A 169 29.622 17.263 3.702 1.00 41.00 A ATOM 818 C LYS A 169 28.801 21.985 7.682 1.00 28.12 A ATOM 819 O LYS A 169 27.785 22.608 7.371 1.00 28.08 A ATOM 820 N TYR A 170 28.826 21.094 8.668 1.00 26.53 A ATOM 821 CA TYR A 170 27.624 20.791 9.434 1.00 26.95 A ATOM 822 CB TYR A 170 27.810 19.476 10.193 1.00 25.03 A ATOM 823 CG TYR A 170 27.898 18.300 9.251 1.00 26.65 A ATOM 824 CD1 TYR A 170 26.745 17.661 8.790 1.00 28.27 A ATOM 825 CE1 TYR A 170 26.814 16.642 7.839 1.00 26.85 A ATOM 826 CD2 TYR A 170 29.127 17.884 8.742 1.00 27.83 A ATOM 827 CE2 TYR A 170 29.209 16.869 7.792 1.00 27.19 A ATOM 828 CZ TYR A 170 28.049 16.254 7.343 1.00 30.02 A ATOM 829 OH TYR A 170 28.130 15.268 6.382 1.00 29.23 A ATOM 830 C TYR A 170 27.229 21.918 10.376 1.00 27.59 A ATOM 831 O TYR A 170 26.045 22.122 10.642 1.00 29.25 A ATOM 832 N ILE A 171 28.208 22.660 10.882 1.00 28.16 A ATOM 833 CA ILE A 171 27.883 23.770 11.763 1.00 29.03 A ATOM 834 CB ILE A 171 29.151 24.435 12.337 1.00 27.51 A ATOM 835 CG2 ILE A 171 28.773 25.705 13.084 1.00 27.97 A ATOM 836 CG1 ILE A 171 29.872 23.458 13.272 1.00 26.70 A ATOM 837 CD1 ILE A 171 31.163 23.996 13.856 1.00 24.07 A ATOM 838 C ILE A 171 27.094 24.796 10.944 1.00 31.41 A ATOM 839 O ILE A 171 26.088 25.335 11.407 1.00 31.69 A ATOM 840 N ARG A 172 27.546 25.047 9.719 1.00 33.21 A ATOM 841 CA ARG A 172 26.874 26.000 8.844 1.00 36.54 A ATOM 842 CB ARG A 172 27.734 26.314 7.616 1.00 37.73 A ATOM 843 CG ARG A 172 29.057 27.011 7.912 1.00 41.65 A ATOM 844 CD ARG A 172 29.708 27.492 6.616 1.00 45.29 A ATOM 845 NE ARG A 172 31.037 28.070 6.812 1.00 48.51 A ATOM 846 CZ ARG A 172 31.314 29.059 7.658 1.00 51.53 A ATOM 847 NH1 ARG A 172 30.355 29.593 8.406 1.00 53.75 A ATOM 848 NH2 ARG A 172 32.553 29.526 7.748 1.00 51.21 A ATOM 849 C ARG A 172 25.528 25.459 8.378 1.00 37.67 A ATOM 850 O ARG A 172 24.550 26.200 8.288 1.00 39.09 A ATOM 851 N LYS A 173 25.481 24.163 8.092 1.00 38.44 A ATOM 852 CA LYS A 173 24.259 23.528 7.619 1.00 39.25 A ATOM 853 CB LYS A 173 24.523 22.061 7.272 1.00 41.89 A ATOM 854 CG LYS A 173 23.279 21.298 6.830 1.00 45.52 A ATOM 855 CD LYS A 173 23.557 19.808 6.653 1.00 49.60 A ATOM 856 CE LYS A 173 24.477 19.530 5.469 1.00 52.63 A ATOM 857 NZ LYS A 173 23.855 19.894 4.160 1.00 54.61 A ATOM 858 C LYS A 173 23.089 23.608 8.595 1.00 39.30 A ATOM 859 O LYS A 173 21.981 23.960 8.201 1.00 39.62 A ATOM 860 N ILE A 174 23.320 23.282 9.863 1.00 37.96 A ATOM 861 CA ILE A 174 22.229 23.314 10.833 1.00 37.36 A ATOM 862 CB ILE A 174 22.159 21.998 11.652 1.00 37.44 A ATOM 863 CG2 ILE A 174 22.058 20.802 10.709 1.00 38.37 A ATOM 864 CG1 ILE A 174 23.397 21.850 12.532 1.00 37.25 A ATOM 865 CD1 ILE A 174 23.355 20.620 13.418 1.00 36.85 A ATOM 866 C ILE A 174 22.259 24.492 11.801 1.00 36.71 A ATOM 867 O ILE A 174 21.448 24.556 12.724 1.00 38.05 A ATOM 868 N GLY A 175 23.185 25.423 11.592 1.00 35.48 A ATOM 869 CA GLY A 175 23.265 26.585 12.462 1.00 35.29 A ATOM 870 C GLY A 175 24.053 26.360 13.737 1.00 35.06 A ATOM 871 O GLY A 175 25.066 27.019 13.970 1.00 37.46 A ATOM 872 N SER A 176 23.581 25.441 14.571 1.00 33.94 A ATOM 873 CA SER A 176 24.253 25.113 15.822 1.00 32.84 A ATOM 874 CB SER A 176 23.938 26.155 16.901 1.00 33.54 A ATOM 875 OG SER A 176 22.599 26.056 17.347 1.00 34.86 A ATOM 876 C SER A 176 23.796 23.731 16.276 1.00 32.34 A ATOM 877 O SER A 176 22.726 23.263 15.884 1.00 32.82 A ATOM 878 N PHE A 177 24.609 23.085 17.103 1.00 29.39 A ATOM 879 CA PHE A 177 24.313 21.743 17.597 1.00 27.20 A ATOM 880 CB PHE A 177 25.621 20.989 17.865 1.00 26.39 A ATOM 881 CG PHE A 177 26.372 20.585 16.622 1.00 26.18 A ATOM 882 CD1 PHE A 177 26.210 21.277 15.426 1.00 25.30 A ATOM 883 CD2 PHE A 177 27.266 19.516 16.662 1.00 26.05 A ATOM 884 CE1 PHE A 177 26.923 20.912 14.290 1.00 26.59 A ATOM 885 CE2 PHE A 177 27.986 19.143 15.532 1.00 26.06 A ATOM 886 CZ PHE A 177 27.815 19.841 14.343 1.00 25.42 A ATOM 887 C PHE A 177 23.500 21.752 18.884 1.00 27.00 A ATOM 888 O PHE A 177 23.704 22.610 19.747 1.00 26.48 A ATOM 889 N ASP A 178 22.578 20.802 19.022 1.00 26.70 A ATOM 890 CA ASP A 178 21.816 20.729 20.260 1.00 26.35 A ATOM 891 CB ASP A 178 20.621 19.773 20.142 1.00 29.90 A ATOM 892 CG ASP A 178 21.020 18.372 19.720 1.00 32.28 A ATOM 893 OD1 ASP A 178 22.157 17.949 20.014 1.00 35.21 A ATOM 894 OD2 ASP A 178 20.179 17.683 19.105 1.00 34.79 A ATOM 895 C ASP A 178 22.810 20.228 21.311 1.00 25.03 A ATOM 896 O ASP A 178 23.974 19.968 20.992 1.00 21.24 A ATOM 897 N GLU A 179 22.361 20.083 22.552 1.00 23.60 A ATOM 898 CA GLU A 179 23.247 19.644 23.619 1.00 25.18 A ATOM 899 CB GLU A 179 22.542 19.770 24.971 1.00 27.60 A ATOM 900 CG GLU A 179 23.324 19.176 26.130 1.00 32.58 A ATOM 901 CD GLU A 179 22.997 19.845 27.449 1.00 35.82 A ATOM 902 OE1 GLU A 179 21.825 20.224 27.645 1.00 35.95 A ATOM 903 OE2 GLU A 179 23.912 19.984 28.291 1.00 38.19 A ATOM 904 C GLU A 179 23.808 18.235 23.450 1.00 24.08 A ATOM 905 O GLU A 179 24.977 17.989 23.756 1.00 22.79 A ATOM 906 N THR A 180 22.983 17.316 22.961 1.00 23.36 A ATOM 907 CA THR A 180 23.412 15.935 22.761 1.00 22.15 A ATOM 908 CB THR A 180 22.224 15.054 22.320 1.00 23.77 A ATOM 909 OG1 THR A 180 21.222 15.075 23.341 1.00 26.37 A ATOM 910 CG2 THR A 180 22.670 13.616 22.088 1.00 22.66 A ATOM 911 C THR A 180 24.533 15.830 21.724 1.00 22.01 A ATOM 912 O THR A 180 25.533 15.141 21.944 1.00 19.87 A ATOM 913 N CYS A 181 24.365 16.511 20.596 1.00 21.21 A ATOM 914 CA CYS A 181 25.372 16.480 19.541 1.00 22.22 A ATOM 915 CB CYS A 181 24.800 17.065 18.250 1.00 24.62 A ATOM 916 SG CYS A 181 23.435 16.080 17.560 1.00 29.50 A ATOM 917 C CYS A 181 26.633 17.232 19.954 1.00 23.07 A ATOM 918 O CYS A 181 27.746 16.827 19.608 1.00 23.95 A ATOM 919 N THR A 182 26.463 18.325 20.695 1.00 22.76 A ATOM 920 CA THR A 182 27.606 19.103 21.161 1.00 21.49 A ATOM 921 CB THR A 182 27.167 20.346 21.978 1.00 21.37 A ATOM 922 OG1 THR A 182 26.459 21.262 21.134 1.00 22.50 A ATOM 923 CG2 THR A 182 28.379 21.046 22.565 1.00 18.36 A ATOM 924 C THR A 182 28.454 18.215 22.071 1.00 21.48 A ATOM 925 O THR A 182 29.669 18.090 21.894 1.00 19.95 A ATOM 926 N ARG A 183 27.798 17.602 23.050 1.00 18.97 A ATOM 927 CA ARG A 183 28.468 16.723 23.996 1.00 19.39 A ATOM 928 CB ARG A 183 27.455 16.140 24.984 1.00 19.46 A ATOM 929 CG ARG A 183 28.030 15.062 25.887 1.00 18.77 A ATOM 930 CD ARG A 183 27.021 14.571 26.925 1.00 21.19 A ATOM 931 NE ARG A 183 26.605 15.642 27.824 1.00 19.46 A ATOM 932 CZ ARG A 183 25.496 16.362 27.679 1.00 20.45 A ATOM 933 NH1 ARG A 183 24.672 16.123 26.666 1.00 19.81 A ATOM 934 NH2 ARG A 183 25.224 17.338 28.539 1.00 17.11 A ATOM 935 C ARG A 183 29.206 15.577 23.302 1.00 20.02 A ATOM 936 O ARG A 183 30.383 15.333 23.573 1.00 19.97 A ATOM 937 N PHE A 184 28.520 14.871 22.409 1.00 19.24 A ATOM 938 CA PHE A 184 29.144 13.746 21.722 1.00 18.04 A ATOM 939 CB PHE A 184 28.158 13.078 20.764 1.00 21.05 A ATOM 940 CG PHE A 184 28.719 11.857 20.098 1.00 22.67 A ATOM 941 CD1 PHE A 184 28.717 10.630 20.754 1.00 22.97 A ATOM 942 CD2 PHE A 184 29.317 11.949 18.850 1.00 19.97 A ATOM 943 CE1 PHE A 184 29.308 9.510 20.176 1.00 23.53 A ATOM 944 CE2 PHE A 184 29.915 10.833 18.263 1.00 24.11 A ATOM 945 CZ PHE A 184 29.910 9.613 18.928 1.00 22.97 A ATOM 946 C PHE A 184 30.403 14.127 20.941 1.00 17.99 A ATOM 947 O PHE A 184 31.461 13.531 21.130 1.00 18.89 A ATOM 948 N TYR A 185 30.292 15.110 20.056 1.00 15.73 A ATOM 949 CA TYR A 185 31.443 15.519 19.265 1.00 15.72 A ATOM 950 CB TYR A 185 30.992 16.413 18.111 1.00 17.33 A ATOM 951 CG TYR A 185 30.364 15.584 17.015 1.00 19.37 A ATOM 952 CD1 TYR A 185 31.159 14.809 16.168 1.00 16.53 A ATOM 953 CE1 TYR A 185 30.590 13.952 15.232 1.00 18.12 A ATOM 954 CD2 TYR A 185 28.976 15.484 16.892 1.00 18.18 A ATOM 955 CE2 TYR A 185 28.398 14.623 15.956 1.00 18.90 A ATOM 956 CZ TYR A 185 29.211 13.861 15.133 1.00 18.41 A ATOM 957 OH TYR A 185 28.650 12.995 14.218 1.00 20.48 A ATOM 958 C TYR A 185 32.544 16.172 20.083 1.00 15.79 A ATOM 959 O TYR A 185 33.720 16.015 19.766 1.00 17.69 A ATOM 960 N THR A 186 32.176 16.887 21.142 1.00 15.68 A ATOM 961 CA THR A 186 33.184 17.504 21.997 1.00 16.03 A ATOM 962 CB THR A 186 32.559 18.403 23.094 1.00 16.62 A ATOM 963 OG1 THR A 186 31.866 19.503 22.481 1.00 14.79 A ATOM 964 CG2 THR A 186 33.656 18.953 24.019 1.00 14.68 A ATOM 965 C THR A 186 33.954 16.375 22.680 1.00 15.59 A ATOM 966 O THR A 186 35.176 16.443 22.823 1.00 13.77 A ATOM 967 N ALA A 187 33.234 15.333 23.097 1.00 14.06 A ATOM 968 CA ALA A 187 33.869 14.196 23.757 1.00 14.74 A ATOM 969 CB ALA A 187 32.810 13.195 24.224 1.00 14.32 A ATOM 970 C ALA A 187 34.875 13.509 22.821 1.00 14.41 A ATOM 971 O ALA A 187 35.972 13.136 23.247 1.00 15.61 A ATOM 972 N GLU A 188 34.516 13.340 21.549 1.00 14.01 A ATOM 973 CA GLU A 188 35.443 12.704 20.615 1.00 13.50 A ATOM 974 CB GLU A 188 34.782 12.449 19.251 1.00 12.85 A ATOM 975 CG GLU A 188 33.622 11.454 19.282 1.00 12.71 A ATOM 976 CD GLU A 188 33.464 10.685 17.979 1.00 15.01 A ATOM 977 OE1 GLU A 188 33.687 11.275 16.899 1.00 13.21 A ATOM 978 OE2 GLU A 188 33.110 9.484 18.031 1.00 17.69 A ATOM 979 C GLU A 188 36.682 13.582 20.436 1.00 13.34 A ATOM 980 O GLU A 188 37.803 13.085 20.408 1.00 14.69 A ATOM 981 N ILE A 189 36.486 14.893 20.326 1.00 13.52 A ATOM 982 CA ILE A 189 37.627 15.787 20.159 1.00 13.35 A ATOM 983 CB ILE A 189 37.169 17.247 19.939 1.00 13.95 A ATOM 984 CG2 ILE A 189 38.381 18.165 19.822 1.00 12.47 A ATOM 985 CG1 ILE A 189 36.302 17.332 18.671 1.00 13.44 A ATOM 986 CD1 ILE A 189 35.588 18.664 18.491 1.00 14.29 A ATOM 987 C ILE A 189 38.530 15.702 21.394 1.00 14.63 A ATOM 988 O ILE A 189 39.753 15.595 21.271 1.00 12.97 A ATOM 989 N VAL A 190 37.927 15.751 22.582 1.00 14.35 A ATOM 990 CA VAL A 190 38.684 15.655 23.832 1.00 13.22 A ATOM 991 CB VAL A 190 37.743 15.690 25.061 1.00 14.28 A ATOM 992 CG1 VAL A 190 38.509 15.267 26.326 1.00 15.08 A ATOM 993 CG2 VAL A 190 37.160 17.082 25.233 1.00 12.08 A ATOM 994 C VAL A 190 39.468 14.338 23.859 1.00 14.61 A ATOM 995 O VAL A 190 40.634 14.304 24.250 1.00 13.72 A ATOM 996 N SER A 191 38.825 13.254 23.432 1.00 15.26 A ATOM 997 CA SER A 191 39.478 11.943 23.421 1.00 16.81 A ATOM 998 CB SER A 191 38.470 10.857 23.041 1.00 16.14 A ATOM 999 OG SER A 191 39.018 9.569 23.238 1.00 16.94 A ATOM 1000 C SER A 191 40.649 11.928 22.441 1.00 16.58 A ATOM 1001 O SER A 191 41.697 11.335 22.713 1.00 13.96 A ATOM 1002 N ALA A 192 40.468 12.586 21.300 1.00 15.26 A ATOM 1003 CA ALA A 192 41.518 12.645 20.292 1.00 14.37 A ATOM 1004 CB ALA A 192 40.989 13.296 19.016 1.00 14.43 A ATOM 1005 C ALA A 192 42.695 13.440 20.845 1.00 16.46 A ATOM 1006 O ALA A 192 43.851 13.038 20.697 1.00 17.96 A ATOM 1007 N LEU A 193 42.401 14.563 21.496 1.00 15.02 A ATOM 1008 CA LEU A 193 43.459 15.392 22.067 1.00 15.42 A ATOM 1009 CB LEU A 193 42.884 16.712 22.600 1.00 12.88 A ATOM 1010 CG LEU A 193 42.445 17.721 21.525 1.00 15.97 A ATOM 1011 CD1 LEU A 193 41.869 18.979 22.190 1.00 13.97 A ATOM 1012 CD2 LEU A 193 43.642 18.088 20.655 1.00 14.58 A ATOM 1013 C LEU A 193 44.211 14.659 23.174 1.00 14.49 A ATOM 1014 O LEU A 193 45.427 14.813 23.310 1.00 16.56 A ATOM 1015 N GLU A 194 43.500 13.870 23.975 1.00 13.96 A ATOM 1016 CA GLU A 194 44.179 13.123 25.032 1.00 14.08 A ATOM 1017 CB GLU A 194 43.190 12.295 25.857 1.00 14.65 A ATOM 1018 CG GLU A 194 43.882 11.301 26.789 1.00 17.09 A ATOM 1019 CD GLU A 194 42.924 10.592 27.730 1.00 19.59 A ATOM 1020 OE1 GLU A 194 41.809 10.237 27.295 1.00 19.25 A ATOM 1021 OE2 GLU A 194 43.302 10.380 28.906 1.00 20.20 A ATOM 1022 C GLU A 194 45.208 12.199 24.386 1.00 13.57 A ATOM 1023 O GLU A 194 46.337 12.093 24.847 1.00 14.23 A ATOM 1024 N TYR A 195 44.822 11.544 23.301 1.00 14.89 A ATOM 1025 CA TYR A 195 45.743 10.642 22.618 1.00 16.58 A ATOM 1026 CB TYR A 195 45.030 9.910 21.488 1.00 17.29 A ATOM 1027 CG TYR A 195 45.956 9.058 20.649 1.00 17.92 A ATOM 1028 CD1 TYR A 195 46.347 7.788 21.077 1.00 17.96 A ATOM 1029 CE1 TYR A 195 47.203 6.996 20.304 1.00 19.77 A ATOM 1030 CD2 TYR A 195 46.445 9.524 19.428 1.00 16.67 A ATOM 1031 CE2 TYR A 195 47.299 8.744 18.650 1.00 18.51 A ATOM 1032 CZ TYR A 195 47.671 7.481 19.094 1.00 20.24 A ATOM 1033 OH TYR A 195 48.506 6.705 18.325 1.00 21.89 A ATOM 1034 C TYR A 195 46.917 11.419 22.035 1.00 16.98 A ATOM 1035 O TYR A 195 48.081 11.047 22.203 1.00 14.61 A ATOM 1036 N LEU A 196 46.599 12.507 21.347 1.00 16.30 A ATOM 1037 CA LEU A 196 47.619 13.328 20.720 1.00 18.15 A ATOM 1038 CB LEU A 196 46.969 14.502 19.982 1.00 18.59 A ATOM 1039 CG LEU A 196 47.834 15.203 18.935 1.00 22.51 A ATOM 1040 CD1 LEU A 196 48.222 14.206 17.841 1.00 20.94 A ATOM 1041 CD2 LEU A 196 47.060 16.375 18.338 1.00 22.98 A ATOM 1042 C LEU A 196 48.592 13.844 21.763 1.00 17.75 A ATOM 1043 O LEU A 196 49.801 13.644 21.649 1.00 18.33 A ATOM 1044 N HIS A 197 48.064 14.495 22.792 1.00 17.12 A ATOM 1045 CA HIS A 197 48.913 15.042 23.842 1.00 18.47 A ATOM 1046 CB HIS A 197 48.069 15.866 24.817 1.00 15.90 A ATOM 1047 CG HIS A 197 47.571 17.152 24.231 1.00 19.15 A ATOM 1048 CD2 HIS A 197 47.830 17.745 23.038 1.00 18.22 A ATOM 1049 ND1 HIS A 197 46.704 17.992 24.897 1.00 17.47 A ATOM 1050 CE1 HIS A 197 46.450 19.047 24.139 1.00 19.74 A ATOM 1051 NE2 HIS A 197 47.119 18.921 23.007 1.00 15.69 A ATOM 1052 C HIS A 197 49.696 13.958 24.572 1.00 19.40 A ATOM 1053 O HIS A 197 50.823 14.192 25.021 1.00 19.42 A ATOM 1054 N GLY A 198 49.106 12.770 24.679 1.00 18.59 A ATOM 1055 CA GLY A 198 49.793 11.675 25.339 1.00 19.60 A ATOM 1056 C GLY A 198 51.075 11.307 24.612 1.00 21.86 A ATOM 1057 O GLY A 198 51.963 10.682 25.186 1.00 23.09 A ATOM 1058 N LYS A 199 51.174 11.687 23.341 1.00 22.81 A ATOM 1059 CA LYS A 199 52.368 11.401 22.549 1.00 24.43 A ATOM 1060 CB LYS A 199 51.990 10.905 21.154 1.00 26.00 A ATOM 1061 CG LYS A 199 51.378 9.520 21.133 1.00 30.98 A ATOM 1062 CD LYS A 199 51.291 9.002 19.708 1.00 36.85 A ATOM 1063 CE LYS A 199 50.832 7.559 19.682 1.00 40.37 A ATOM 1064 NZ LYS A 199 51.646 6.691 20.581 1.00 43.48 A ATOM 1065 C LYS A 199 53.253 12.631 22.414 1.00 23.88 A ATOM 1066 O LYS A 199 54.144 12.669 21.568 1.00 24.97 A ATOM 1067 N GLY A 200 52.997 13.638 23.243 1.00 24.00 A ATOM 1068 CA GLY A 200 53.790 14.853 23.203 1.00 22.12 A ATOM 1069 C GLY A 200 53.665 15.632 21.907 1.00 22.14 A ATOM 1070 O GLY A 200 54.632 16.231 21.439 1.00 22.41 A ATOM 1071 N ILE A 201 52.475 15.630 21.320 1.00 20.00 A ATOM 1072 CA ILE A 201 52.252 16.355 20.080 1.00 18.93 A ATOM 1073 CB ILE A 201 51.784 15.414 18.955 1.00 19.70 A ATOM 1074 CG2 ILE A 201 51.414 16.226 17.716 1.00 20.12 A ATOM 1075 CG1 ILE A 201 52.880 14.395 18.636 1.00 20.03 A ATOM 1076 CD1 ILE A 201 52.408 13.258 17.745 1.00 22.75 A ATOM 1077 C ILE A 201 51.193 17.425 20.270 1.00 19.87 A ATOM 1078 O ILE A 201 50.121 17.161 20.817 1.00 20.08 A ATOM 1079 N ILE A 202 51.508 18.633 19.815 1.00 19.94 A ATOM 1080 CA ILE A 202 50.601 19.772 19.891 1.00 20.45 A ATOM 1081 CB ILE A 202 51.352 21.040 20.356 1.00 22.21 A ATOM 1082 CG2 ILE A 202 50.381 22.220 20.470 1.00 22.67 A ATOM 1083 CG1 ILE A 202 52.033 20.775 21.700 1.00 24.19 A ATOM 1084 CD1 ILE A 202 52.914 21.920 22.169 1.00 25.39 A ATOM 1085 C ILE A 202 50.105 19.999 18.464 1.00 20.71 A ATOM 1086 O ILE A 202 50.910 20.067 17.538 1.00 19.48 A ATOM 1087 N HIS A 203 48.795 20.108 18.270 1.00 18.65 A ATOM 1088 CA HIS A 203 48.280 20.319 16.919 1.00 18.02 A ATOM 1089 CB HIS A 203 46.775 20.057 16.874 1.00 16.31 A ATOM 1090 CG HIS A 203 46.199 20.136 15.495 1.00 18.36 A ATOM 1091 CD2 HIS A 203 46.043 21.186 14.655 1.00 16.42 A ATOM 1092 ND1 HIS A 203 45.759 19.026 14.806 1.00 19.50 A ATOM 1093 CE1 HIS A 203 45.359 19.389 13.600 1.00 17.64 A ATOM 1094 NE2 HIS A 203 45.522 20.694 13.483 1.00 20.87 A ATOM 1095 C HIS A 203 48.589 21.738 16.405 1.00 18.92 A ATOM 1096 O HIS A 203 49.073 21.906 15.282 1.00 16.21 A ATOM 1097 N ARG A 204 48.301 22.744 17.232 1.00 18.60 A ATOM 1098 CA ARG A 204 48.552 24.157 16.914 1.00 19.81 A ATOM 1099 CB ARG A 204 49.998 24.365 16.458 1.00 21.61 A ATOM 1100 CG ARG A 204 51.024 24.137 17.550 1.00 23.82 A ATOM 1101 CD ARG A 204 52.323 24.870 17.252 1.00 27.62 A ATOM 1102 NE ARG A 204 52.932 24.449 15.994 1.00 29.43 A ATOM 1103 CZ ARG A 204 54.125 24.861 15.572 1.00 33.10 A ATOM 1104 NH1 ARG A 204 54.835 25.706 16.311 1.00 32.12 A ATOM 1105 NH2 ARG A 204 54.614 24.426 14.418 1.00 30.25 A ATOM 1106 C ARG A 204 47.624 24.830 15.905 1.00 20.03 A ATOM 1107 O ARG A 204 47.711 26.038 15.698 1.00 20.88 A ATOM 1108 N ASP A 205 46.755 24.071 15.255 1.00 18.96 A ATOM 1109 CA ASP A 205 45.828 24.692 14.325 1.00 17.90 A ATOM 1110 CB ASP A 205 46.418 24.741 12.914 1.00 18.95 A ATOM 1111 CG ASP A 205 45.655 25.688 12.008 1.00 20.36 A ATOM 1112 OD1 ASP A 205 44.939 26.560 12.545 1.00 20.35 A ATOM 1113 OD2 ASP A 205 45.772 25.573 10.771 1.00 22.49 A ATOM 1114 C ASP A 205 44.500 23.956 14.328 1.00 19.60 A ATOM 1115 O ASP A 205 43.876 23.751 13.287 1.00 21.53 A ATOM 1116 N LEU A 206 44.063 23.569 15.521 1.00 18.53 A ATOM 1117 CA LEU A 206 42.813 22.851 15.667 1.00 19.18 A ATOM 1118 CB LEU A 206 42.693 22.295 17.087 1.00 18.94 A ATOM 1119 CG LEU A 206 41.511 21.358 17.346 1.00 23.10 A ATOM 1120 CD1 LEU A 206 41.615 20.142 16.436 1.00 23.01 A ATOM 1121 CD2 LEU A 206 41.504 20.933 18.808 1.00 22.97 A ATOM 1122 C LEU A 206 41.639 23.772 15.361 1.00 19.05 A ATOM 1123 O LEU A 206 41.556 24.880 15.886 1.00 19.25 A ATOM 1124 N LYS A 207 40.740 23.307 14.500 1.00 17.54 A ATOM 1125 CA LYS A 207 39.564 24.081 14.110 1.00 18.60 A ATOM 1126 CB LYS A 207 39.980 25.248 13.196 1.00 18.98 A ATOM 1127 CG LYS A 207 40.786 24.817 11.982 1.00 18.20 A ATOM 1128 CD LYS A 207 41.246 26.000 11.139 1.00 21.42 A ATOM 1129 CE LYS A 207 42.223 25.537 10.062 1.00 23.21 A ATOM 1130 NZ LYS A 207 42.561 26.604 9.084 1.00 29.61 A ATOM 1131 C LYS A 207 38.566 23.181 13.388 1.00 18.18 A ATOM 1132 O LYS A 207 38.921 22.100 12.915 1.00 18.11 A ATOM 1133 N PRO A 208 37.298 23.614 13.293 1.00 20.26 A ATOM 1134 CD PRO A 208 36.713 24.833 13.882 1.00 18.79 A ATOM 1135 CA PRO A 208 36.272 22.814 12.616 1.00 19.67 A ATOM 1136 CB PRO A 208 35.063 23.742 12.608 1.00 19.45 A ATOM 1137 CG PRO A 208 35.231 24.509 13.891 1.00 21.81 A ATOM 1138 C PRO A 208 36.674 22.372 11.209 1.00 21.04 A ATOM 1139 O PRO A 208 36.264 21.307 10.751 1.00 21.19 A ATOM 1140 N GLU A 209 37.474 23.188 10.528 1.00 21.69 A ATOM 1141 CA GLU A 209 37.928 22.872 9.170 1.00 22.64 A ATOM 1142 CB GLU A 209 38.644 24.084 8.558 1.00 23.65 A ATOM 1143 CG GLU A 209 39.253 23.825 7.185 1.00 27.24 A ATOM 1144 CD GLU A 209 40.155 24.958 6.716 1.00 29.40 A ATOM 1145 OE1 GLU A 209 39.660 26.094 6.553 1.00 29.68 A ATOM 1146 OE2 GLU A 209 41.363 24.711 6.511 1.00 30.07 A ATOM 1147 C GLU A 209 38.879 21.668 9.159 1.00 22.28 A ATOM 1148 O GLU A 209 38.955 20.933 8.170 1.00 21.36 A ATOM 1149 N ASN A 210 39.600 21.490 10.263 1.00 19.90 A ATOM 1150 CA ASN A 210 40.574 20.412 10.436 1.00 19.44 A ATOM 1151 CB ASN A 210 41.744 20.912 11.287 1.00 20.07 A ATOM 1152 CG ASN A 210 42.746 21.698 10.479 1.00 25.77 A ATOM 1153 OD1 ASN A 210 43.571 22.427 11.029 1.00 26.73 A ATOM 1154 ND2 ASN A 210 42.687 21.548 9.158 1.00 25.15 A ATOM 1155 C ASN A 210 40.005 19.151 11.078 1.00 18.63 A ATOM 1156 O ASN A 210 40.712 18.154 11.234 1.00 18.29 A ATOM 1157 N ILE A 211 38.739 19.202 11.469 1.00 16.31 A ATOM 1158 CA ILE A 211 38.090 18.058 12.085 1.00 15.49 A ATOM 1159 CB ILE A 211 37.336 18.488 13.354 1.00 15.40 A ATOM 1160 CG2 ILE A 211 36.582 17.311 13.950 1.00 14.59 A ATOM 1161 CG1 ILE A 211 38.342 19.046 14.365 1.00 15.91 A ATOM 1162 CD1 ILE A 211 37.720 19.669 15.590 1.00 15.98 A ATOM 1163 C ILE A 211 37.131 17.485 11.059 1.00 17.26 A ATOM 1164 O ILE A 211 35.995 17.947 10.926 1.00 18.16 A ATOM 1165 N LEU A 212 37.599 16.486 10.317 1.00 15.97 A ATOM 1166 CA LEU A 212 36.784 15.875 9.274 1.00 17.08 A ATOM 1167 CB LEU A 212 37.685 15.249 8.202 1.00 17.78 A ATOM 1168 CG LEU A 212 38.785 16.157 7.640 1.00 18.92 A ATOM 1169 CD1 LEU A 212 39.476 15.450 6.485 1.00 22.09 A ATOM 1170 CD2 LEU A 212 38.188 17.482 7.166 1.00 19.91 A ATOM 1171 C LEU A 212 35.843 14.825 9.837 1.00 18.35 A ATOM 1172 O LEU A 212 35.957 14.433 11.002 1.00 19.39 A ATOM 1173 N LEU A 213 34.915 14.368 9.000 1.00 17.84 A ATOM 1174 CA LEU A 213 33.942 13.362 9.403 1.00 19.94 A ATOM 1175 CB LEU A 213 32.556 14.004 9.487 1.00 20.84 A ATOM 1176 CG LEU A 213 32.396 15.059 10.583 1.00 20.31 A ATOM 1177 CD1 LEU A 213 31.124 15.837 10.367 1.00 22.75 A ATOM 1178 CD2 LEU A 213 32.379 14.378 11.940 1.00 23.93 A ATOM 1179 C LEU A 213 33.914 12.187 8.426 1.00 20.98 A ATOM 1180 O LEU A 213 33.743 12.379 7.218 1.00 19.55 A ATOM 1181 N ASN A 214 34.088 10.970 8.935 1.00 20.44 A ATOM 1182 CA ASN A 214 34.055 9.814 8.049 1.00 23.77 A ATOM 1183 CB ASN A 214 34.745 8.596 8.674 1.00 25.30 A ATOM 1184 CG ASN A 214 34.077 8.127 9.948 1.00 32.04 A ATOM 1185 OD1 ASN A 214 32.908 8.422 10.206 1.00 34.43 A ATOM 1186 ND2 ASN A 214 34.818 7.369 10.752 1.00 33.85 A ATOM 1187 C ASN A 214 32.618 9.466 7.693 1.00 24.07 A ATOM 1188 O ASN A 214 31.672 10.113 8.150 1.00 19.94 A ATOM 1189 N GLU A 215 32.459 8.433 6.879 1.00 25.77 A ATOM 1190 CA GLU A 215 31.138 8.003 6.445 1.00 28.69 A ATOM 1191 CB GLU A 215 31.275 6.796 5.513 1.00 31.98 A ATOM 1192 CG GLU A 215 29.970 6.334 4.896 1.00 40.22 A ATOM 1193 CD GLU A 215 30.182 5.312 3.795 1.00 44.27 A ATOM 1194 OE1 GLU A 215 30.817 4.268 4.065 1.00 46.46 A ATOM 1195 OE2 GLU A 215 29.716 5.556 2.660 1.00 46.13 A ATOM 1196 C GLU A 215 30.188 7.673 7.601 1.00 28.41 A ATOM 1197 O GLU A 215 28.971 7.769 7.447 1.00 28.52 A ATOM 1198 N ASP A 216 30.737 7.287 8.752 1.00 26.77 A ATOM 1199 CA ASP A 216 29.914 6.953 9.917 1.00 27.28 A ATOM 1200 CB ASP A 216 30.538 5.795 10.696 1.00 31.27 A ATOM 1201 CG ASP A 216 30.390 4.466 9.979 1.00 37.61 A ATOM 1202 OD1 ASP A 216 29.274 4.170 9.499 1.00 39.45 A ATOM 1203 OD2 ASP A 216 31.382 3.710 9.902 1.00 41.84 A ATOM 1204 C ASP A 216 29.697 8.135 10.862 1.00 26.37 A ATOM 1205 O ASP A 216 29.136 7.984 11.950 1.00 25.73 A ATOM 1206 N MET A 217 30.156 9.306 10.441 1.00 23.02 A ATOM 1207 CA MET A 217 30.015 10.527 11.218 1.00 21.83 A ATOM 1208 CB MET A 217 28.537 10.789 11.517 1.00 23.24 A ATOM 1209 CG MET A 217 27.742 11.186 10.274 1.00 22.98 A ATOM 1210 SD MET A 217 28.464 12.616 9.430 1.00 27.57 A ATOM 1211 CE MET A 217 27.679 13.974 10.332 1.00 26.68 A ATOM 1212 C MET A 217 30.844 10.618 12.502 1.00 21.51 A ATOM 1213 O MET A 217 30.474 11.323 13.440 1.00 18.62 A ATOM 1214 N HIS A 218 31.957 9.892 12.544 1.00 20.10 A ATOM 1215 CA HIS A 218 32.873 9.964 13.678 1.00 19.86 A ATOM 1216 CB HIS A 218 33.482 8.594 13.977 1.00 20.21 A ATOM 1217 CG HIS A 218 32.551 7.667 14.698 1.00 22.40 A ATOM 1218 CD2 HIS A 218 31.910 6.547 14.287 1.00 21.27 A ATOM 1219 ND1 HIS A 218 32.177 7.863 16.011 1.00 19.59 A ATOM 1220 CE1 HIS A 218 31.348 6.902 16.379 1.00 21.88 A ATOM 1221 NE2 HIS A 218 31.168 6.091 15.351 1.00 22.08 A ATOM 1222 C HIS A 218 33.947 10.921 13.172 1.00 19.10 A ATOM 1223 O HIS A 218 34.1701 11.004 11.965 1.00 20.31 A ATOM 1224 N ILE A 219 34.617 11.638 14.067 1.00 17.21 A ATOM 1225 CA ILE A 219 35.628 12.586 13.618 1.00 15.26 A ATOM 1226 CB ILE A 219 35.987 13.614 14.716 1.00 15.38 A ATOM 1227 CG2 ILE A 219 34.722 14.305 15.221 1.00 14.58 A ATOM 1228 CG1 ILE A 219 36.734 12.919 15.864 1.00 14.46 A ATOM 1229 CD1 ILE A 219 37.279 13.885 16.911 1.00 13.74 A ATOM 1230 C ILE A 219 36.929 11.944 13.161 1.00 16.21 A ATOM 1231 O ILE A 219 37.238 10.799 13.500 1.00 15.88 A ATOM 1232 N GLN A 220 37.677 12.711 12.378 1.00 15.62 A ATOM 1233 CA GLN A 220 38.980 12.316 11.876 1.00 17.84 A ATOM 1234 CB GLN A 220 38.872 11.595 10.525 1.00 20.00 A ATOM 1235 CG GLN A 220 38.463 10.129 10.659 1.00 26.97 A ATOM 1236 CD GLN A 220 38.648 9.343 9.372 1.00 29.95 A ATOM 1237 OE1 GLN A 220 37.968 9.590 8.373 1.00 33.12 A ATOM 1238 NE2 GLN A 220 39.578 8.393 9.389 1.00 30.47 A ATOM 1239 C GLN A 220 39.757 13.610 11.735 1.00 17.00 A ATOM 1240 O GLN A 220 39.609 14.339 10.751 1.00 18.27 A ATOM 1241 N ILE A 221 40.566 13.906 12.746 1.00 14.34 A ATOM 1242 CA ILE A 221 41.361 15.120 12.753 1.00 14.46 A ATOM 1243 CB ILE A 221 41.867 15.416 14.175 1.00 12.30 A ATOM 1244 CG2 ILE A 221 42.764 16.656 14.167 1.00 14.78 A ATOM 1245 CG1 ILE A 221 40.660 15.613 15.102 1.00 13.92 A ATOM 1246 CD1 ILE A 221 41.003 15.901 16.543 1.00 15.06 A ATOM 1247 C ILE A 221 42.536 14.996 11.783 1.00 15.44 A ATOM 1248 O ILE A 221 43.106 13.915 11.613 1.00 13.93 A ATOM 1249 N THR A 222 42.877 16.101 11.127 1.00 15.36 A ATOM 1250 CA THR A 222 43.980 16.098 10.174 1.00 17.52 A ATOM 1251 CB THR A 222 43.470 15.836 8.750 1.00 19.92 A ATOM 1252 OG1 THR A 222 44.587 15.637 7.875 1.00 18.78 A ATOM 1253 CG2 THR A 222 42.630 17.018 8.257 1.00 18.16 A ATOM 1254 C THR A 222 44.735 17.428 10.192 1.00 19.60 A ATOM 1255 O THR A 222 44.509 18.257 11.084 1.00 18.59 A ATOM 1256 N ASP A 223 45.630 17.610 9.216 1.00 18.69 A ATOM 1257 CA ASP A 223 46.440 18.825 9.069 1.00 20.12 A ATOM 1258 CB ASP A 223 45.532 20.065 9.108 1.00 23.51 A ATOM 1259 CG ASP A 223 46.248 21.335 8.670 1.00 27.09 A ATOM 1260 OD1 ASP A 223 47.283 21.227 7.975 1.00 26.28 A ATOM 1261 OD2 ASP A 223 45.765 22.438 9.009 1.00 26.15 A ATOM 1262 C ASP A 223 47.516 18.913 10.150 1.00 21.73 A ATOM 1263 O ASP A 223 47.439 19.751 11.055 1.00 22.76 A ATOM 1264 N PHE A 224 48.535 18.063 10.027 1.00 20.75 A ATOM 1265 CA PHE A 224 49.611 17.988 11.009 1.00 20.11 A ATOM 1266 CB PHE A 224 49.805 16.527 11.424 1.00 20.62 A ATOM 1267 CG PHE A 224 48.682 15.991 12.263 1.00 21.41 A ATOM 1268 CD1 PHE A 224 48.598 16.312 13.614 1.00 23.05 A ATOM 1269 CD2 PHE A 224 47.681 15.212 11.693 1.00 22.27 A ATOM 1270 CE1 PHE A 224 47.528 15.868 14.389 1.00 23.30 A ATOM 1271 CE2 PHE A 224 46.606 14.763 12.457 1.00 21.11 A ATOM 1272 CZ PHE A 224 46.530 15.093 13.807 1.00 22.02 A ATOM 1273 C PHE A 224 50.957 18.583 10.619 1.00 20.45 A ATOM 1274 O PHE A 224 51.905 18.547 11.407 1.00 20.73 A ATOM 1275 N GLY A 225 51.049 19.125 9.412 1.00 22.02 A ATOM 1276 CA GLY A 225 52.301 19.713 8.981 1.00 22.66 A ATOM 1277 C GLY A 225 52.742 20.822 9.920 1.00 24.99 A ATOM 1278 O GLY A 225 53.939 21.041 10.122 1.00 24.52 A ATOM 1279 N THR A 226 51.779 21.524 10.508 1.00 23.50 A ATOM 1280 CA THR A 226 52.106 22.613 11.416 1.00 25.16 A ATOM 1281 CB THR A 226 51.199 23.829 11.160 1.00 24.76 A ATOM 1282 OG1 THR A 226 49.831 23.410 11.113 1.00 22.68 A ATOM 1283 CG2 THR A 226 51.571 24.490 9.834 1.00 25.00 A ATOM 1284 C THR A 226 52.046 22.233 12.894 1.00 25.79 A ATOM 1285 O THR A 226 52.019 23.100 13.768 1.00 24.54 A ATOM 1286 N ALA A 227 52.037 20.935 13.173 1.00 24.97 A ATOM 1287 CA ALA A 227 52.004 20.475 14.550 1.00 25.49 A ATOM 1288 CB ALA A 227 51.659 18.993 14.607 1.00 22.85 A ATOM 1289 C ALA A 227 53.384 20.715 15.149 1.00 27.70 A ATOM 1290 O ALA A 227 54.331 21.047 14.435 1.00 26.60 A ATOM 1291 N LYS A 228 53.491 20.558 16.461 1.00 28.53 A ATOM 1292 CA LYS A 228 54.760 20.745 17.149 1.00 32.12 A ATOM 1293 CB LYS A 228 54.699 21.974 18.054 1.00 33.81 A ATOM 1294 CG LYS A 228 56.007 22.294 18.765 1.00 41.23 A ATOM 1295 CD LYS A 228 57.082 22.725 17.768 1.00 47.57 A ATOM 1296 CE LYS A 228 58.401 23.056 18.462 1.00 49.82 A ATOM 1297 NZ LYS A 228 59.459 23.425 17.480 1.00 51.49 A ATOM 1298 C LYS A 228 55.019 19.504 17.985 1.00 33.25 A ATOM 1299 O LYS A 228 54.190 19.129 18.815 1.00 33.70 A ATOM 1300 N VAL A 229 56.159 18.860 17.756 1.00 33.64 A ATOM 1301 CA VAL A 229 56.516 17.661 18.501 1.00 34.66 A ATOM 1302 CB VAL A 229 57.248 16.646 17.609 1.00 33.50 A ATOM 1303 CG1 VAL A 229 57.619 15.419 18.415 1.00 32.34 A ATOM 1304 CG2 VAL A 229 56.370 16.264 16.436 1.00 34.25 A ATOM 1305 C VAL A 229 57.420 18.035 19.668 1.00 37.57 A ATOM 1306 O VAL A 229 58.581 18.392 19.474 1.00 35.91 A ATOM 1307 N LEU A 230 56.877 17.948 20.878 1.00 40.57 A ATOM 1308 CA LEU A 230 57.615 18.289 22.088 1.00 46.10 A ATOM 1309 CB LEU A 230 56.654 18.417 23.270 1.00 44.71 A ATOM 1310 CG LEU A 230 55.627 19.545 23.207 1.00 44.50 A ATOM 1311 CD1 LEU A 230 54.673 19.430 24.383 1.00 44.39 A ATOM 1312 CD2 LEU A 230 56.340 20.885 23.214 1.00 44.81 A ATOM 1313 C LEU A 230 58.695 17.279 22.440 1.00 50.42 A ATOM 1314 O LEU A 230 58.603 16.104 22.089 1.00 51.64 A ATOM 1315 N SER A 231 59.717 17.756 23.145 1.00 55.81 A ATOM 1316 CA SER A 231 60.824 16.914 23.583 1.00 61.14 A ATOM 1317 CB SER A 231 62.077 17.200 22.750 1.00 61.27 A ATOM 1318 OG SER A 231 62.444 18.568 22.823 1.00 62.85 A ATOM 1319 C SER A 231 61.124 17.126 25.071 1.00 64.65 A ATOM 1320 O SER A 231 61.392 16.164 25.794 1.00 65.70 A ATOM 1321 N PRO A 232 61.081 18.387 25.549 1.00 67.54 A ATOM 1322 CD PRO A 232 60.854 19.651 24.823 1.00 68.60 A ATOM 1323 CA PRO A 232 61.358 18.655 26.966 1.00 68.74 A ATOM 1324 CB PRO A 232 61.109 20.158 27.086 1.00 68.83 A ATOM 1325 CG PRO A 232 61.505 20.666 25.737 1.00 68.96 A ATOM 1326 C PRO A 232 60.460 17.846 27.899 1.00 69.17 A ATOM 1327 O PRO A 232 59.335 17.494 27.541 1.00 69.94 A ATOM 1328 N ALA A 237 57.424 23.198 27.637 1.00 80.06 A ATOM 1329 CA ALA A 237 56.783 23.047 26.335 1.00 79.29 A ATOM 1330 CB ALA A 237 55.275 22.907 26.512 1.00 78.64 A ATOM 1331 C ALA A 237 57.092 24.239 25.433 1.00 79.07 A ATOM 1332 O ALA A 237 56.250 25.113 25.249 1.00 79.47 A ATOM 1333 N ALA A 238 58.297 24.280 24.871 1.00 78.57 A ATOM 1334 CA ALA A 238 58.683 25.383 23.992 1.00 78.50 A ATOM 1335 CB ALA A 238 60.186 25.347 23.728 1.00 78.50 A ATOM 1336 C ALA A 238 57.920 25.327 22.673 1.00 78.15 A ATOM 1337 O ALA A 238 57.243 24.341 22.375 1.00 77.96 A ATOM 1338 N ALA A 239 58.027 26.393 21.887 1.00 77.28 A ATOM 1339 CA ALA A 239 57.338 26.452 20.603 1.00 76.27 A ATOM 1340 CB ALA A 239 55.849 26.489 20.827 1.00 76.61 A ATOM 1341 C ALA A 239 57.766 27.667 19.793 1.00 75.38 A ATOM 1342 O ALA A 239 58.955 27.955 19.700 1.00 75.89 A ATOM 1343 N ASN A 240 56.781 28.357 19.214 1.00 73.95 A ATOM 1344 CA ASN A 240 56.967 29.553 18.389 1.00 71.07 A ATOM 1345 CB ASN A 240 58.151 30.400 18.874 1.00 71.47 A ATOM 1346 CG ASN A 240 59.459 30.055 18.174 1.00 72.06 A ATOM 1347 OD1 ASN A 240 59.575 30.149 16.943 1.00 72.03 A ATOM 1348 ND2 ASN A 240 60.470 29.665 18.964 1.00 71.91 A ATOM 1349 C ASN A 240 57.188 29.178 16.928 1.00 69.41 A ATOM 1350 O ASN A 240 57.480 28.024 16.624 1.00 70.09 A ATOM 1351 N ALA A 241 57.055 30.165 16.038 1.00 66.62 A ATOM 1352 CA ALA A 241 57.246 30.013 14.585 1.00 63.94 A ATOM 1353 C ALA A 241 55.952 30.080 13.772 1.00 60.63 A ATOM 1354 O ALA A 241 55.840 30.880 12.845 1.00 61.29 A ATOM 1355 CB ALA A 241 57.979 28.704 14.246 1.00 65.23 A ATOM 1356 N PHE A 242 54.984 29.236 14.113 1.00 56.72 A ATOM 1357 CA PHE A 242 53.712 29.196 13.394 1.00 52.53 A ATOM 1358 CB PHE A 242 53.419 27.767 12.923 1.00 49.14 A ATOM 1359 CG PHE A 242 52.040 27.590 12.354 1.00 47.38 A ATOM 1360 CD1 PHE A 242 51.731 28.067 11.085 1.00 47.69 A ATOM 1361 CD2 PHE A 242 51.038 26.975 13.102 1.00 45.45 A ATOM 1362 CE1 PHE A 242 50.445 27.937 10.565 1.00 46.75 A ATOM 1363 CE2 PHE A 242 49.751 26.840 12.594 1.00 45.41 A ATOM 1364 CZ PHE A 242 49.453 27.323 11.322 1.00 46.55 A ATOM 1365 C PHE A 242 52.534 29.688 14.229 1.00 50.08 A ATOM 1366 O PHE A 242 52.502 29.505 15.444 1.00 49.86 A ATOM 1367 N VAL A 243 51.566 30.305 13.557 1.00 47.67 A ATOM 1368 CA VAL A 243 50.355 30.809 14.200 1.00 46.21 A ATOM 1369 CB VAL A 243 50.340 32.352 14.258 1.00 47.36 A ATOM 1370 CG1 VAL A 243 49.012 32.844 14.825 1.00 47.54 A ATOM 1371 CG2 VAL A 243 51.497 32.842 15.109 1.00 48.50 A ATOM 1372 C VAL A 243 49.150 30.342 13.389 1.00 44.12 A ATOM 1373 O VAL A 243 48.956 30.765 12.247 1.00 44.46 A ATOM 1374 N GLY A 244 48.348 29.467 13.985 1.00 40.48 A ATOM 1375 CA GLY A 244 47.176 28.941 13.306 1.00 37.65 A ATOM 1376 C GLY A 244 46.101 29.960 12.964 1.00 35.39 A ATOM 1377 O GLY A 244 46.313 31.168 13.065 1.00 35.92 A ATOM 1378 N THR A 245 44.936 29.463 12.560 1.00 33.30 A ATOM 1379 CA THR A 245 43.813 30.312 12.184 1.00 30.20 A ATOM 1380 CB THR A 245 42.593 29.450 11.829 1.00 32.00 A ATOM 1381 OG1 THR A 245 42.952 28.573 10.755 1.00 32.81 A ATOM 1382 CG2 THR A 245 41.419 30.319 11.390 1.00 28.34 A ATOM 1383 C THR A 245 43.476 31.296 13.296 1.00 27.96 A ATOM 1384 O THR A 245 43.212 30.907 14.434 1.00 25.46 A ATOM 1385 N ALA A 246 43.486 32.576 12.938 1.00 25.22 A ATOM 1386 CA ALA A 246 43.247 33.675 13.867 1.00 23.27 A ATOM 1387 CB ALA A 246 42.956 34.955 13.082 1.00 22.94 A ATOM 1388 C ALA A 246 42.178 33.475 14.934 1.00 21.27 A ATOM 1389 O ALA A 246 42.431 33.705 16.114 1.00 20.93 A ATOM 1390 N GLN A 247 40.988 33.047 14.536 1.00 19.67 A ATOM 1391 CA GLN A 247 39.911 32.886 15.504 1.00 20.17 A ATOM 1392 CB GLN A 247 38.608 32.535 14.779 1.00 21.89 A ATOM 1393 CG GLN A 247 38.522 33.076 13.355 1.00 26.18 A ATOM 1394 CD GLN A 247 37.220 33.794 13.064 1.00 27.30 A ATOM 1395 OE1 GLN A 247 36.172 33.447 13.605 1.00 30.13 A ATOM 1396 NE2 GLN A 247 37.278 34.792 12.189 1.00 28.70 A ATOM 1397 C GLN A 247 40.181 31.849 16.595 1.00 19.43 A ATOM 1398 O GLN A 247 39.546 31.883 17.648 1.00 18.93 A ATOM 1399 N TYR A 248 41.132 30.948 16.359 1.00 18.60 A ATOM 1400 CA TYR A 248 41.441 29.896 17.329 1.00 19.20 A ATOM 1401 CB TYR A 248 41.333 28.529 16.642 1.00 17.53 A ATOM 1402 CG TYR A 248 40.013 28.362 15.927 1.00 19.32 A ATOM 1403 CD1 TYR A 248 38.859 28.010 16.625 1.00 17.69 A ATOM 1404 CE1 TYR A 248 37.617 27.976 15.990 1.00 18.18 A ATOM 1405 CD2 TYR A 248 39.897 28.664 14.569 1.00 16.87 A ATOM 1406 CE2 TYR A 248 38.665 28.635 13.924 1.00 19.17 A ATOM 1407 CZ TYR A 248 37.527 28.295 14.643 1.00 19.46 A ATOM 1408 OH TYR A 248 36.299 28.311 14.023 1.00 18.98 A ATOM 1409 C TYR A 248 42.810 30.039 17.993 1.00 20.42 A ATOM 1410 O TYR A 248 43.208 29.191 18.792 1.00 19.19 A ATOM 1411 N VAL A 249 43.523 31.114 17.673 1.00 20.20 A ATOM 1412 CA VAL A 249 44.841 31.343 18.251 1.00 20.91 A ATOM 1413 CB VAL A 249 45.542 32.532 17.570 1.00 21.18 A ATOM 1414 CG1 VAL A 249 46.821 32.896 18.317 1.00 22.45 A ATOM 1415 CG2 VAL A 249 45.862 32.170 16.139 1.00 24.01 A ATOM 1416 C VAL A 249 44.764 31.606 19.750 1.00 21.52 A ATOM 1417 O VAL A 249 43.915 32.368 20.216 1.00 22.72 A ATOM 1418 N SER A 250 45.654 30.965 20.503 1.00 20.70 A ATOM 1419 CA SER A 250 45.697 31.133 21.951 1.00 21.65 A ATOM 1420 CB SER A 250 46.370 29.919 22.613 1.00 22.02 A ATOM 1421 OG SER A 250 47.692 29.725 22.132 1.00 22.12 A ATOM 1422 C SER A 250 46.476 32.402 22.280 1.00 22.13 A ATOM 1423 O SER A 250 47.332 32.828 21.511 1.00 22.77 A ATOM 1424 N PRO A 251 46.180 33.029 23.425 1.00 22.23 A ATOM 1425 CD PRO A 251 45.163 32.684 24.433 1.00 22.97 A ATOM 1426 CA PRO A 251 46.893 34.254 23.800 1.00 22.52 A ATOM 1427 CB PRO A 251 46.233 34.650 25.127 1.00 23.06 A ATOM 1428 CG PRO A 251 45.726 33.329 25.676 1.00 22.55 A ATOM 1429 C PRO A 251 48.414 34.115 23.907 1.00 22.15 A ATOM 1430 O PRO A 251 49.143 35.047 23.563 1.00 22.62 A ATOM 1431 N GLU A 252 48.901 32.966 24.367 1.00 20.69 A ATOM 1432 CA GLU A 252 50.347 32.772 24.500 1.00 21.40 A ATOM 1433 CB GLU A 252 50.673 31.382 25.071 1.00 20.59 A ATOM 1434 CG GLU A 252 49.993 30.232 24.352 1.00 21.91 A ATOM 1435 CD GLU A 252 48.691 29.822 25.014 1.00 21.51 A ATOM 1436 OE1 GLU A 252 47.989 30.707 25.550 1.00 21.46 A ATOM 1437 OE2 GLU A 252 48.367 28.613 24.993 1.00 20.23 A ATOM 1438 C GLU A 252 51.071 32.970 23.167 1.00 22.99 A ATOM 1439 O GLU A 252 52.191 33.480 23.136 1.00 23.17 A ATOM 1440 N LEU A 253 50.441 32.576 22.064 1.00 23.00 A ATOM 1441 CA LEU A 253 51.068 32.753 20.758 1.00 25.62 A ATOM 1442 CB LEU A 253 50.277 32.029 19.669 1.00 26.75 A ATOM 1443 CG LEU A 253 50.743 30.620 19.296 1.00 31.87 A ATOM 1444 CD1 LEU A 253 50.433 29.651 20.422 1.00 31.81 A ATOM 1445 CD2 LEU A 253 50.044 30.179 18.015 1.00 31.86 A ATOM 1446 C LEU A 253 51.201 34.228 20.371 1.00 26.94 A ATOM 1447 O LEU A 253 52.107 34.601 19.626 1.00 27.09 A ATOM 1448 N LEU A 254 50.297 35.059 20.877 1.00 25.83 A ATOM 1449 CA LEU A 254 50.297 36.485 20.564 1.00 27.26 A ATOM 1450 CB LEU A 254 48.858 37.006 20.564 1.00 25.84 A ATOM 1451 CG LEU A 254 47.882 36.290 19.621 1.00 24.69 A ATOM 1452 CD1 LEU A 254 46.459 36.724 19.932 1.00 23.64 A ATOM 1453 CD2 LEU A 254 48.236 36.597 18.177 1.00 24.24 A ATOM 1454 C LEU A 254 51.134 37.314 21.537 1.00 30.62 A ATOM 1455 O LEU A 254 51.633 38.383 21.187 1.00 32.35 A ATOM 1456 N THR A 255 51.292 36.821 22.758 1.00 32.47 A ATOM 1457 CA THR A 255 52.056 37.547 23.759 1.00 36.70 A ATOM 1458 CB THR A 255 51.368 37.478 25.127 1.00 34.51 A ATOM 1459 OG1 THR A 255 51.188 36.106 25.494 1.00 35.49 A ATOM 1460 CG2 THR A 255 50.013 38.166 25.077 1.00 33.40 A ATOM 1461 C THR A 255 53.477 37.035 23.910 1.00 40.09 A ATOM 1462 O THR A 255 54.430 37.793 23.772 1.00 43.69 A ATOM 1463 N GLU A 256 53.617 35.747 24.189 1.00 44.77 A ATOM 1464 CA GLU A 256 54.932 35.144 24.382 1.00 49.15 A ATOM 1465 CB GLU A 256 54.866 34.143 25.534 1.00 51.24 A ATOM 1466 CG GLU A 256 54.514 34.786 26.862 1.00 56.03 A ATOM 1467 CD GLU A 256 54.053 33.780 27.893 1.00 58.83 A ATOM 1468 OE1 GLU A 256 54.766 32.776 28.107 1.00 62.13 A ATOM 1469 OE2 GLU A 256 52.979 33.996 28.494 1.00 60.34 A ATOM 1470 C GLU A 256 55.475 34.456 23.137 1.00 50.09 A ATOM 1471 O GLU A 256 56.616 33.995 23.127 1.00 50.42 A ATOM 1472 N LYS A 257 54.658 34.389 22.090 1.00 51.21 A ATOM 1473 CA LYS A 257 55.064 33.746 20.845 1.00 51.22 A ATOM 1474 CB LYS A 257 56.244 34.502 20.227 1.00 53.28 A ATOM 1475 CG LYS A 257 56.558 34.125 18.790 1.00 55.19 A ATOM 1476 CD LYS A 257 57.709 34.961 18.253 1.00 57.52 A ATOM 1477 CE LYS A 257 57.952 34.694 16.777 1.00 58.52 A ATOM 1478 NZ LYS A 257 58.290 33.268 16.515 1.00 60.88 A ATOM 1479 C LYS A 257 55.467 32.302 21.138 1.00 50.74 A ATOM 1480 O LYS A 257 56.432 31.790 20.577 1.00 52.26 A ATOM 1481 N SER A 258 54.721 31.654 22.027 1.00 48.07 A ATOM 1482 CA SER A 258 54.999 30.273 22.402 1.00 46.87 A ATOM 1483 CB SER A 258 55.590 30.229 23.812 1.00 48.88 A ATOM 1484 OG SER A 258 54.741 30.892 24.734 1.00 53.14 A ATOM 1485 C SER A 258 53.735 29.415 22.342 1.00 44.07 A ATOM 1486 O SER A 258 52.617 29.932 22.417 1.00 44.17 A ATOM 1487 N ALA A 259 53.917 28.105 22.204 1.00 38.30 A ATOM 1488 CA ALA A 259 52.793 27.180 22.127 1.00 34.73 A ATOM 1489 CB ALA A 259 52.551 26.779 20.684 1.00 34.16 A ATOM 1490 C ALA A 259 53.042 25.940 22.977 1.00 32.34 A ATOM 1491 O ALA A 259 54.172 25.459 23.086 1.00 31.81 A ATOM 1492 N CYS A 260 51.975 25.428 23.579 1.00 28.58 A ATOM 1493 CA CYS A 260 52.056 24.244 24.425 1.00 26.27 A ATOM 1494 CB CYS A 260 52.183 24.654 25.892 1.00 26.53 A ATOM 1495 SG CYS A 260 50.846 25.739 26.469 1.00 32.91 A ATOM 1496 C CYS A 260 50.786 23.435 24.224 1.00 22.83 A ATOM 1497 O CYS A 260 49.892 23.856 23.495 1.00 22.14 A ATOM 1498 N LYS A 261 50.706 22.277 24.868 1.00 20.02 A ATOM 1499 CA LYS A 261 49.526 21.434 24.744 1.00 20.65 A ATOM 1500 CB LYS A 261 49.619 20.243 25.696 1.00 23.28 A ATOM 1501 CG LYS A 261 50.716 19.253 25.347 1.00 27.44 A ATOM 1502 CD LYS A 261 50.732 18.117 26.350 1.00 29.98 A ATOM 1503 CE LYS A 261 51.922 17.203 26.134 1.00 32.34 A ATOM 1504 NZ LYS A 261 51.940 16.121 27.153 1.00 33.28 A ATOM 1505 C LYS A 261 48.268 22.229 25.062 1.00 19.20 A ATOM 1506 O LYS A 261 47.253 22.092 24.387 1.00 18.08 A ATOM 1507 N SER A 262 48.358 23.068 26.089 1.00 16.92 A ATOM 1508 CA SER A 262 47.235 23.883 26.534 1.00 18.13 A ATOM 1509 CB SER A 262 47.644 24.698 27.770 1.00 18.27 A ATOM 1510 OG SER A 262 46.517 25.258 28.421 1.00 22.53 A ATOM 1511 C SER A 262 46.736 24.811 25.424 1.00 16.77 A ATOM 1512 O SER A 262 45.591 25.254 25.450 1.00 15.69 A ATOM 1513 N SER A 263 47.595 25.118 24.456 1.00 16.44 A ATOM 1514 CA SER A 263 47.175 25.970 23.347 1.00 16.89 A ATOM 1515 CB SER A 263 48.340 26.228 22.382 1.00 18.49 A ATOM 1516 OG SER A 263 49.402 26.909 23.031 1.00 22.10 A ATOM 1517 C SER A 263 46.040 25.257 22.612 1.00 17.79 A ATOM 1518 O SER A 263 45.099 25.898 22.148 1.00 17.57 A ATOM 1519 N ASP A 264 46.119 23.928 22.517 1.00 16.30 A ATOM 1520 CA ASP A 264 45.069 23.166 21.836 1.00 16.72 A ATOM 1521 CB ASP A 264 45.483 21.704 21.620 1.00 15.92 A ATOM 1522 CG ASP A 264 46.544 21.539 20.548 1.00 17.93 A ATOM 1523 OD1 ASP A 264 46.642 22.412 19.661 1.00 16.78 A ATOM 1524 OD2 ASP A 264 47.265 20.515 20.579 1.00 16.64 A ATOM 1525 C ASP A 264 43.773 23.194 22.646 1.00 17.67 A ATOM 1526 O ASP A 264 42.681 23.197 22.076 1.00 18.27 A ATOM 1527 N LEU A 265 43.898 23.205 23.974 1.00 15.49 A ATOM 1528 CA LEU A 265 42.730 23.232 24.849 1.00 14.75 A ATOM 1529 CB LEU A 265 43.147 23.038 26.313 1.00 11.38 A ATOM 1530 CG LEU A 265 43.711 21.641 26.621 1.00 14.04 A ATOM 1531 CD1 LEU A 265 44.249 21.579 28.052 1.00 13.96 A ATOM 1532 CD2 LEU A 265 42.619 20.603 26.416 1.00 11.62 A ATOM 1533 C LEU A 265 41.999 24.557 24.675 1.00 15.13 A ATOM 1534 O LEU A 265 40.777 24.620 24.785 1.00 16.75 A ATOM 1535 N TRP A 266 42.746 25.622 24.405 1.00 16.08 A ATOM 1536 CA TRP A 266 42.118 26.918 24.184 1.00 16.96 A ATOM 1537 CB TRP A 266 43.176 28.015 24.023 1.00 17.28 A ATOM 1538 CG TRP A 266 42.618 29.326 23.521 1.00 20.54 A ATOM 1539 CD2 TRP A 266 42.313 30.490 24.301 1.00 20.07 A ATOM 1540 CE2 TRP A 266 41.782 31.459 23.417 1.00 20.46 A ATOM 1541 CE3 TRP A 266 42.435 30.810 25.660 1.00 20.68 A ATOM 1542 CD1 TRP A 266 42.270 29.631 22.231 1.00 19.53 A ATOM 1543 NE1 TRP A 266 41.769 30.908 22.163 1.00 19.61 A ATOM 1544 CZ2 TRP A 266 41.372 32.727 23.850 1.00 20.90 A ATOM 1545 CZ3 TRP A 266 42.026 32.073 26.091 1.00 19.45 A ATOM 1546 CH2 TRP A 266 41.501 33.015 25.185 1.00 20.71 A ATOM 1547 C TRP A 266 41.284 26.795 22.913 1.00 17.22 A ATOM 1548 O TRP A 266 40.139 27.240 22.863 1.00 18.03 A ATOM 1549 N ALA A 267 41.863 26.181 21.886 1.00 17.50 A ATOM 1550 CA ALA A 267 41.155 25.990 20.626 1.00 16.16 A ATOM 1551 CB ALA A 267 42.050 25.290 19.621 1.00 14.28 A ATOM 1552 C ALA A 267 39.901 25.159 20.891 1.00 16.28 A ATOM 1553 O ALA A 267 38.835 25.436 20.346 1.00 16.46 A ATOM 1554 N LEU A 268 40.031 24.144 21.739 1.00 16.57 A ATOM 1555 CA LEU A 268 38.890 23.299 22.084 1.00 17.03 A ATOM 1556 CB LEU A 268 39.292 22.260 23.139 1.00 15.35 A ATOM 1557 CG LEU A 268 38.158 21.429 23.754 1.00 19.00 A ATOM 1558 CD1 LEU A 268 37.505 20.578 22.678 1.00 16.17 A ATOM 1559 CD2 LEU A 268 38.718 20.537 24.881 1.00 17.49 A ATOM 1560 C LEU A 268 37.766 24.179 22.628 1.00 15.72 A ATOM 1561 O LEU A 268 36.603 24.031 22.247 1.00 15.28 A ATOM 1562 N GLY A 269 38.119 25.099 23.520 1.00 14.34 A ATOM 1563 CA GLY A 269 37.124 25.989 24.092 1.00 13.39 A ATOM 1564 C GLY A 269 36.406 26.808 23.031 1.00 14.94 A ATOM 1565 O GLY A 269 35.193 27.014 23.114 1.00 14.76 A ATOM 1566 N CYS A 270 37.146 27.279 22.030 1.00 13.86 A ATOM 1567 CA CYS A 270 36.539 28.061 20.958 1.00 16.80 A ATOM 1568 CB CYS A 270 37.611 28.634 20.023 1.00 15.97 A ATOM 1569 SG CYS A 270 38.751 29.810 20.780 1.00 20.48 A ATOM 1570 C CYS A 270 35.598 27.175 20.140 1.00 17.50 A ATOM 1571 O CYS A 270 34.516 27.604 19.741 1.00 18.38 A ATOM 1572 N ILE A 271 36.022 25.939 19.887 1.00 16.99 A ATOM 1573 CA ILE A 271 35.221 25.004 19.104 1.00 16.66 A ATOM 1574 CB ILE A 271 36.038 23.741 18.778 1.00 16.53 A ATOM 1575 CG2 ILE A 271 35.155 22.694 18.102 1.00 16.34 A ATOM 1576 CG1 ILE A 271 37.222 24.129 17.882 1.00 15.59 A ATOM 1577 CD1 ILE A 271 38.239 23.018 17.690 1.00 14.88 A ATOM 1578 C ILE A 271 33.920 24.626 19.809 1.00 16.74 A ATOM 1579 O ILE A 271 32.865 24.576 19.179 1.00 17.12 A ATOM 1580 N ILE A 272 33.990 24.357 21.111 1.00 16.13 A ATOM 1581 CA ILE A 272 32.785 24.021 21.862 1.00 18.30 A ATOM 1582 CB ILE A 272 33.097 23.747 23.346 1.00 17.77 A ATOM 1583 CG2 ILE A 272 31.796 23.666 24.152 1.00 17.96 A ATOM 1584 CG1 ILE A 272 33.877 22.437 23.481 1.00 19.55 A ATOM 1585 CD1 ILE A 272 34.446 22.217 24.886 1.00 18.64 A ATOM 1586 C ILE A 272 31.824 25.207 21.776 1.00 19.51 A ATOM 1587 O ILE A 272 30.624 25.037 21.554 1.00 20.44 A ATOM 1588 N TYR A 273 32.362 26.409 21.947 1.00 18.52 A ATOM 1589 CA TYR A 273 31.553 27.615 21.881 1.00 20.48 A ATOM 1590 CB TYR A 273 32.418 28.847 22.162 1.00 18.98 A ATOM 1591 CG TYR A 273 31.663 30.161 22.125 1.00 20.26 A ATOM 1592 CD1 TYR A 273 31.229 30.709 20.916 1.00 20.67 A ATOM 1593 CE1 TYR A 273 30.536 31.917 20.880 1.00 20.98 A ATOM 1594 CD2 TYR A 273 31.383 30.857 23.302 1.00 19.82 A ATOM 1595 CE2 TYR A 273 30.691 32.062 23.280 1.00 20.62 A ATOM 1596 CZ TYR A 273 30.271 32.587 22.067 1.00 21.15 A ATOM 1597 OH TYR A 273 29.588 33.776 22.049 1.00 21.86 A ATOM 1598 C TYR A 273 30.902 27.730 20.507 1.00 21.54 A ATOM 1599 O TYR A 273 29.719 28.049 20.401 1.00 22.80 A ATOM 1600 N GLN A 274 31.676 27.454 19.461 1.00 21.05 A ATOM 1601 CA GLN A 274 31.176 27.538 18.095 1.00 21.48 A ATOM 1602 CB GLN A 274 32.323 27.341 17.097 1.00 21.41 A ATOM 1603 CG GLN A 274 31.934 27.596 15.645 1.00 23.15 A ATOM 1604 CD GLN A 274 33.131 27.588 14.706 1.00 24.80 A ATOM 1605 OE1 GLN A 274 34.276 27.446 15.139 1.00 22.51 A ATOM 1606 NE2 GLN A 274 32.870 27.750 13.413 1.00 22.96 A ATOM 1607 C GLN A 274 30.076 26.517 17.828 1.00 21.51 A ATOM 1608 O GLN A 274 29.123 26.806 17.108 1.00 20.50 A ATOM 1609 N LEU A 275 30.207 25.324 18.403 1.00 21.44 A ATOM 1610 CA LEU A 275 29.196 24.282 18.208 1.00 20.95 A ATOM 1611 CB LEU A 275 29.645 22.958 18.846 1.00 19.11 A ATOM 1612 CG LEU A 275 30.775 22.182 18.159 1.00 21.43 A ATOM 1613 CD1 LEU A 275 31.118 20.936 18.963 1.00 17.64 A ATOM 1614 CD2 LEU A 275 30.342 21.795 16.754 1.00 20.34 A ATOM 1615 C LEU A 275 27.860 24.697 18.815 1.00 21.32 A ATOM 1616 O LEU A 275 26.802 24.461 18.229 1.00 19.75 A ATOM 1617 N VAL A 276 27.921 25.322 19.987 1.00 19.10 A ATOM 1618 CA VAL A 276 26.724 25.750 20.702 1.00 22.47 A ATOM 1619 CB VAL A 276 27.011 25.882 22.217 1.00 20.87 A ATOM 1620 CG1 VAL A 276 25.742 26.291 22.957 1.00 19.68 A ATOM 1621 CG2 VAL A 276 27.550 24.558 22.766 1.00 19.43 A ATOM 1622 C VAL A 276 26.127 27.075 20.211 1.00 23.89 A ATOM 1623 O VAL A 276 24.910 27.199 20.070 1.00 24.90 A ATOM 1624 N ALA A 277 26.983 28.062 19.965 1.00 24.56 A ATOM 1625 CA ALA A 277 26.533 29.374 19.518 1.00 24.72 A ATOM 1626 CB ALA A 277 27.504 30.444 19.999 1.00 24.36 A ATOM 1627 C ALA A 277 26.378 29.458 18.005 1.00 25.76 A ATOM 1628 O ALA A 277 25.577 30.242 17.502 1.00 26.39 A ATOM 1629 N GLY A 278 27.142 28.651 17.280 1.00 25.13 A ATOM 1630 CA GLY A 278 27.062 28.673 15.834 1.00 25.58 A ATOM 1631 C GLY A 278 28.163 29.524 15.231 1.00 26.50 A ATOM 1632 O GLY A 278 28.374 29.510 14.015 1.00 28.17 A ATOM 1633 N LEU A 279 28.866 30.262 16.086 1.00 24.44 A ATOM 1634 CA LEU A 279 29.962 31.130 15.656 1.00 25.21 A ATOM 1635 CB LEU A 279 29.468 32.575 15.500 1.00 25.78 A ATOM 1636 CG LEU A 279 28.364 32.899 14.490 1.00 28.17 A ATOM 1637 CD1 LEU A 279 27.922 34.344 14.684 1.00 26.60 A ATOM 1638 CD2 LEU A 279 28.862 32.670 13.071 1.00 26.52 A ATOM 1639 C LEU A 279 31.093 31.116 16.687 1.00 23.47 A ATOM 1640 O LEU A 279 30.848 30.994 17.882 1.00 24.44 A ATOM 1641 N PRO A 280 32.349 31.239 16.236 1.00 23.35 A ATOM 1642 CD PRO A 280 32.831 31.404 14.855 1.00 22.26 A ATOM 1643 CA PRO A 280 33.464 31.239 17.189 1.00 23.81 A ATOM 1644 CB PRO A 280 34.692 31.293 16.282 1.00 23.24 A ATOM 1645 CG PRO A 280 34.189 32.020 15.073 1.00 24.89 A ATOM 1646 C PRO A 280 33.353 32.444 18.137 1.00 22.69 A ATOM 1647 O PRO A 280 32.750 33.457 17.788 1.00 22.11 A ATOM 1648 N PRO A 281 33.939 32.344 19.345 1.00 23.06 A ATOM 1649 CD PRO A 281 34.810 31.223 19.734 1.00 21.37 A ATOM 1650 CA PRO A 281 33.935 33.375 20.395 1.00 23.67 A ATOM 1651 CB PRO A 281 34.781 32.751 21.509 1.00 24.89 A ATOM 1652 CG PRO A 281 34.749 31.287 21.219 1.00 25.24 A ATOM 1653 C PRO A 281 34.481 34.752 20.017 1.00 23.75 A ATOM 1654 O PRO A 281 33.869 35.781 20.317 1.00 21.02 A ATOM 1655 N PHE A 282 35.644 34.763 19.379 1.00 22.17 A ATOM 1656 CA PHE A 282 36.293 36.007 18.998 1.00 23.16 A ATOM 1657 CB PHE A 282 37.765 35.943 19.406 1.00 21.01 A ATOM 1658 CG PHE A 282 37.975 35.482 20.822 1.00 22.66 A ATOM 1659 CD1 PHE A 282 37.806 36.361 21.888 1.00 20.06 A ATOM 1660 CD2 PHE A 282 38.291 34.151 21.093 1.00 20.72 A ATOM 1661 CE1 PHE A 282 37.947 35.921 23.206 1.00 22.66 A ATOM 1662 CE2 PHE A 282 38.433 33.702 22.405 1.00 20.97 A ATOM 1663 CZ PHE A 282 38.261 34.590 23.466 1.00 19.58 A ATOM 1664 C PHE A 282 36.169 36.263 17.503 1.00 24.39 A ATOM 1665 O PHE A 282 36.802 35.585 16.694 1.00 25.80 A ATOM 1666 N ARG A 283 35.355 37.248 17.142 1.00 24.99 A ATOM 1667 CA ARG A 283 35.141 37.594 15.741 1.00 26.33 A ATOM 1668 CB ARG A 283 33.721 37.209 15.316 1.00 28.91 A ATOM 1669 CG ARG A 283 33.293 35.808 15.724 1.00 30.27 A ATOM 1670 CD ARG A 283 31.904 35.493 15.188 1.00 33.36 A ATOM 1671 NE ARG A 283 30.890 36.392 15.733 1.00 32.76 A ATOM 1672 CZ ARG A 283 30.372 36.287 16.952 1.00 34.79 A ATOM 1673 NH1 ARG A 283 30.767 35.317 17.768 1.00 35.77 A ATOM 1674 NH2 ARG A 283 29.458 37.156 17.359 1.00 36.12 A ATOM 1675 C ARG A 283 35.328 39.096 15.544 1.00 26.47 A ATOM 1676 O ARG A 283 35.029 39.888 16.438 1.00 26.28 A ATOM 1677 N ALA A 284 35.818 39.486 14.373 1.00 26.70 A ATOM 1678 CA ALA A 284 36.033 40.899 14.079 1.00 27.84 A ATOM 1679 CB ALA A 284 37.188 41.442 14.914 1.00 26.24 A ATOM 1680 C ALA A 284 36.327 41.077 12.602 1.00 28.35 A ATOM 1681 O ALA A 284 36.560 40.101 11.891 1.00 29.91 A ATOM 1682 N GLY A 285 36.332 42.329 12.153 1.00 29.29 A ATOM 1683 CA GLY A 285 36.577 42.631 10.753 1.00 29.52 A ATOM 1684 C GLY A 285 37.893 42.156 10.168 1.00 30.12 A ATOM 1685 O GLY A 285 37.974 41.862 8.976 1.00 30.60 A ATOM 1686 N ASN A 286 38.939 42.097 10.983 1.00 28.49 A ATOM 1687 CA ASN A 286 40.231 41.644 10.489 1.00 26.71 A ATOM 1688 CB ASN A 286 41.050 42.825 9.945 1.00 26.11 A ATOM 1689 CG ASN A 286 41.310 43.900 10.990 1.00 27.83 A ATOM 1690 OD1 ASN A 286 41.877 43.631 12.049 1.00 27.84 A ATOM 1691 ND2 ASN A 286 40.908 45.131 10.685 1.00 25.95 A ATOM 1692 C ASN A 286 40.997 40.924 11.584 1.00 26.03 A ATOM 1693 O ASN A 286 40.540 40.851 12.723 1.00 25.66 A ATOM 1694 N GLU A 287 42.162 40.391 11.239 1.00 24.81 A ATOM 1695 CA GLU A 287 42.965 39.662 12.206 1.00 27.59 A ATOM 1696 CB GLU A 287 44.145 38.985 11.510 1.00 30.17 A ATOM 1697 CG GLU A 287 43.776 37.632 10.931 1.00 38.21 A ATOM 1698 CD GLU A 287 44.900 36.998 10.140 1.00 41.86 A ATOM 1699 OE1 GLU A 287 46.061 37.036 10.608 1.00 43.08 A ATOM 1700 OE2 GLU A 287 44.612 36.449 9.052 1.00 45.22 A ATOM 1701 C GLU A 287 43.459 40.485 13.383 1.00 25.05 A ATOM 1702 O GLU A 287 43.382 40.030 14.521 1.00 26.41 A ATOM 1703 N TYR A 288 43.966 41.685 13.122 1.00 23.04 A ATOM 1704 CA TYR A 288 44.460 42.528 14.205 1.00 22.34 A ATOM 1705 CB TYR A 288 44.867 43.913 13.691 1.00 21.07 A ATOM 1706 CG TYR A 288 45.275 44.858 14.805 1.00 21.07 A ATOM 1707 CD1 TYR A 288 46.533 44.762 15.405 1.00 21.23 A ATOM 1708 CE1 TYR A 288 46.891 45.588 16.475 1.00 20.43 A ATOM 1709 CD2 TYR A 288 44.380 45.809 15.302 1.00 22.32 A ATOM 1710 CE2 TYR A 288 44.725 46.637 16.373 1.00 23.28 A ATOM 1711 CZ TYR A 288 45.981 46.518 16.953 1.00 22.96 A ATOM 1712 OH TYR A 288 46.316 47.313 18.024 1.00 23.18 A ATOM 1713 C TYR A 288 43.402 42.698 15.288 1.00 21.38 A ATOM 1714 O TYR A 288 43.710 42.616 16.473 1.00 22.09 A ATOM 1715 N LEU A 289 42.159 42.939 14.874 1.00 21.88 A ATOM 1716 CA LEU A 289 41.055 43.130 15.811 1.00 21.98 A ATOM 1717 CB LEU A 289 39.821 43.673 15.078 1.00 22.90 A ATOM 1718 CG LEU A 289 39.896 45.130 14.601 1.00 26.52 A ATOM 1719 CD1 LEU A 289 38.706 45.436 13.696 1.00 26.55 A ATOM 1720 CD2 LEU A 289 39.914 46.071 15.807 1.00 23.13 A ATOM 1721 C LEU A 289 40.686 41.849 16.560 1.00 21.24 A ATOM 1722 O LEU A 289 40.256 41.897 17.715 1.00 20.72 A ATOM 1723 N ILE A 290 40.843 40.708 15.900 1.00 19.62 A ATOM 1724 CA ILE A 290 40.538 39.433 16.533 1.00 18.54 A ATOM 1725 CB ILE A 290 40.560 38.281 15.509 1.00 18.52 A ATOM 1726 CG2 ILE A 290 40.503 36.934 16.234 1.00 17.63 A ATOM 1727 CG1 ILE A 290 39.378 38.429 14.545 1.00 18.88 A ATOM 1728 CD1 ILE A 290 39.421 37.483 13.357 1.00 19.81 A ATOM 1729 C ILE A 290 41.578 39.167 17.618 1.00 19.09 A ATOM 1730 O ILE A 290 41.236 38.788 18.737 1.00 18.20 A ATOM 1731 N PHE A 291 42.849 39.376 17.286 1.00 18.76 A ATOM 1732 CA PHE A 291 43.925 39.156 18.247 1.00 20.75 A ATOM 1733 CB PHE A 291 45.286 39.434 17.606 1.00 20.71 A ATOM 1734 CG PHE A 291 45.644 38.480 16.503 1.00 22.92 A ATOM 1735 CD1 PHE A 291 45.065 37.214 16.443 1.00 22.98 A ATOM 1736 CD2 PHE A 291 46.588 38.830 15.543 1.00 22.91 A ATOM 1737 CE1 PHE A 291 45.423 36.310 15.440 1.00 24.51 A ATOM 1738 CE2 PHE A 291 46.954 37.931 14.535 1.00 25.54 A ATOM 1739 CZ PHE A 291 46.370 36.670 14.485 1.00 23.29 A ATOM 1740 C PHE A 291 43.739 40.061 19.451 1.00 21.72 A ATOM 1741 O PHE A 291 43.992 39.671 20.593 1.00 22.32 A ATOM 1742 N GLN A 292 43.284 41.275 19.178 1.00 23.27 A ATOM 1743 CA GLN A 292 43.055 42.264 20.216 1.00 24.01 A ATOM 1744 CB GLN A 292 42.574 43.559 19.562 1.00 25.77 A ATOM 1745 CG GLN A 292 42.577 44.773 20.447 1.00 28.45 A ATOM 1746 CD GLN A 292 42.469 46.057 19.638 1.00 29.83 A ATOM 1747 OE1 GLN A 292 41.520 46.244 18.872 1.00 27.16 A ATOM 1748 NE2 GLN A 292 43.449 46.944 19.799 1.00 27.61 A ATOM 1749 C GLN A 292 42.018 41.733 21.204 1.00 22.97 A ATOM 1750 O GLN A 292 42.200 41.832 22.415 1.00 21.64 A ATOM 1751 N LYS A 293 40.937 41.154 20.687 1.00 21.82 A ATOM 1752 CA LYS A 293 39.895 40.612 21.558 1.00 22.18 A ATOM 1753 CB LYS A 293 38.664 40.223 20.740 1.00 22.69 A ATOM 1754 CG LYS A 293 37.919 41.407 20.153 1.00 25.78 A ATOM 1755 CD LYS A 293 36.651 40.961 19.429 1.00 27.88 A ATOM 1756 CE LYS A 293 35.857 42.161 18.926 1.00 30.85 A ATOM 1757 NZ LYS A 293 34.612 41.750 18.214 1.00 32.98 A ATOM 1758 C LYS A 293 40.398 39.398 22.343 1.00 21.20 A ATOM 1759 O LYS A 293 40.041 39.204 23.509 1.00 22.01 A ATOM 1760 N ILE A 294 41.226 38.583 21.702 1.00 19.91 A ATOM 1761 CA ILE A 294 41.774 37.394 22.347 1.00 20.28 A ATOM 1762 CB ILE A 294 42.631 36.575 21.349 1.00 18.98 A ATOM 1763 CG2 ILE A 294 43.481 35.550 22.098 1.00 17.70 A ATOM 1764 CG1 ILE A 294 41.716 35.897 20.318 1.00 17.93 A ATOM 1765 CD1 ILE A 294 42.467 35.237 19.178 1.00 16.21 A ATOM 1766 C ILE A 294 42.618 37.727 23.587 1.00 21.94 A ATOM 1767 O ILE A 294 42.366 37.199 24.673 1.00 20.86 A ATOM 1768 N ILE A 295 43.610 38.600 23.439 1.00 21.88 A ATOM 1769 CA ILE A 295 44.461 38.934 24.582 1.00 24.25 A ATOM 1770 CB ILE A 295 45.668 39.805 24.175 1.00 23.93 A ATOM 1771 CG2 ILE A 295 46.514 39.066 23.140 1.00 24.61 A ATOM 1772 CG1 ILE A 295 45.189 41.151 23.637 1.00 24.58 A ATOM 1773 CD1 ILE A 295 46.317 42.149 23.433 1.00 26.69 A ATOM 1774 C ILE A 295 43.720 39.636 25.717 1.00 24.80 A ATOM 1775 O ILE A 295 44.214 39.687 26.842 1.00 24.76 A ATOM 1776 N LYS A 296 42.539 40.173 25.425 1.00 25.33 A ATOM 1777 CA LYS A 296 41.743 40.853 26.444 1.00 26.80 A ATOM 1778 CB LYS A 296 41.178 42.170 25.894 1.00 27.39 A ATOM 1779 CG LYS A 296 42.240 43.141 25.413 1.00 31.79 A ATOM 1780 CD LYS A 296 41.634 44.410 24.826 1.00 35.56 A ATOM 1781 CE LYS A 296 41.009 45.283 25.900 1.00 39.29 A ATOM 1782 NZ LYS A 296 40.564 46.603 25.357 1.00 41.72 A ATOM 1783 C LYS A 296 40.593 39.958 26.893 1.00 25.50 A ATOM 1784 O LYS A 296 39.770 40.361 27.713 1.00 24.02 A ATOM 1785 N LEU A 297 40.550 38.742 26.349 1.00 25.67 A ATOM 1786 CA LEU A 297 39.500 37.777 26.666 1.00 25.16 A ATOM 1787 CB LEU A 297 39.632 37.285 28.111 1.00 24.80 A ATOM 1788 CG LEU A 297 38.766 36.068 28.460 1.00 26.43 A ATOM 1789 CD1 LEU A 297 39.238 34.852 27.646 1.00 26.70 A ATOM 1790 CD2 LEU A 297 38.856 35.777 29.951 1.00 24.84 A ATOM 1791 C LEU A 297 38.151 38.459 26.467 1.00 25.11 A ATOM 1792 O LEU A 297 37.261 38.378 27.309 1.00 25.28 A ATOM 1793 N GLU A 298 38.007 39.127 25.331 1.00 24.98 A ATOM 1794 CA GLU A 298 36.786 39.847 25.023 1.00 25.31 A ATOM 1795 CB GLU A 298 37.143 41.139 24.291 1.00 27.13 A ATOM 1796 CG GLU A 298 35.991 42.092 24.108 1.00 31.28 A ATOM 1797 CD GLU A 298 36.419 43.362 23.410 1.00 34.40 A ATOM 1798 OE1 GLU A 298 37.348 44.027 23.918 1.00 35.90 A ATOM 1799 OE2 GLU A 298 35.832 43.693 22.359 1.00 36.16 A ATOM 1800 C GLU A 298 35.766 39.057 24.207 1.00 23.79 A ATOM 1801 O GLU A 298 35.832 39.017 22.979 1.00 24.35 A ATOM 1802 N TYR A 299 34.825 38.427 24.902 1.00 23.45 A ATOM 1803 CA TYR A 299 33.760 37.663 24.265 1.00 23.98 A ATOM 1804 CB TYR A 299 34.264 36.304 23.755 1.00 20.13 A ATOM 1805 CG TYR A 299 34.348 35.233 24.828 1.00 21.17 A ATOM 1806 CD1 TYR A 299 35.336 35.279 25.810 1.00 19.32 A ATOM 1807 CE1 TYR A 299 35.389 34.332 26.826 1.00 19.30 A ATOM 1808 CD2 TYR A 299 33.410 34.201 24.888 1.00 18.96 A ATOM 1809 CE2 TYR A 299 33.456 33.243 25.907 1.00 19.41 A ATOM 1810 CZ TYR A 299 34.449 33.321 26.870 1.00 18.79 A ATOM 1811 OH TYR A 299 34.511 32.401 27.881 1.00 18.77 A ATOM 1812 C TYR A 299 32.699 37.437 25.331 1.00 25.20 A ATOM 1813 O TYR A 299 32.942 37.681 26.506 1.00 26.46 A ATOM 1814 N ASP A 300 31.522 36.981 24.927 1.00 26.94 A ATOM 1815 CA ASP A 300 30.467 36.710 25.891 1.00 30.60 A ATOM 1816 CB ASP A 300 29.665 37.981 26.179 1.00 35.86 A ATOM 1817 CG ASP A 300 29.228 38.687 24.923 1.00 42.04 A ATOM 1818 OD1 ASP A 300 28.450 38.088 24.149 1.00 45.98 A ATOM 1819 OD2 ASP A 300 29.666 39.840 24.707 1.00 45.69 A ATOM 1820 C ASP A 300 29.564 35.608 25.363 1.00 29.26 A ATOM 1821 O ASP A 300 29.590 35.299 24.172 1.00 28.64 A ATOM 1822 N PHE A 301 28.778 35.011 26.253 1.00 28.96 A ATOM 1823 CA PHE A 301 27.884 33.924 25.871 1.00 30.48 A ATOM 1824 CB PHE A 301 27.818 32.854 26.968 1.00 29.17 A ATOM 1825 CG PHE A 301 29.147 32.279 27.356 1.00 29.29 A ATOM 1826 CD1 PHE A 301 29.978 32.949 28.245 1.00 27.31 A ATOM 1827 CD2 PHE A 301 29.560 31.050 26.845 1.00 27.89 A ATOM 1828 CE1 PHE A 301 31.205 32.403 28.625 1.00 28.83 A ATOM 1829 CE2 PHE A 301 30.781 30.498 27.217 1.00 28.05 A ATOM 1830 CZ PHE A 301 31.605 31.175 28.110 1.00 28.27 A ATOM 1831 C PHE A 301 26.459 34.384 25.619 1.00 32.20 A ATOM 1832 O PHE A 301 25.946 35.261 26.317 1.00 32.36 A ATOM 1833 N PRO A 302 25.798 33.804 24.607 1.00 33.29 A ATOM 1834 CD PRO A 302 26.313 32.943 23.529 1.00 34.04 A ATOM 1835 CA PRO A 302 24.415 34.199 24.341 1.00 35.24 A ATOM 1836 CB PRO A 302 24.144 33.608 22.959 1.00 34.01 A ATOM 1837 CG PRO A 302 25.041 32.413 22.921 1.00 35.48 A ATOM 1838 C PRO A 302 23.567 33.561 25.444 1.00 37.39 A ATOM 1839 O PRO A 302 23.935 32.518 25.986 1.00 38.49 A ATOM 1840 N ALA A 303 22.447 34.188 25.783 1.00 39.36 A ATOM 1841 CA ALA A 303 21.572 33.692 26.843 1.00 40.65 A ATOM 1842 CB ALA A 303 20.280 34.506 26.862 1.00 41.66 A ATOM 1843 C ALA A 303 21.238 32.197 26.814 1.00 41.25 A ATOM 1844 O ALA A 303 21.253 31.537 27.854 1.00 43.16 A ATOM 1845 N ALA A 304 20.945 31.665 25.631 1.00 41.04 A ATOM 1846 CA ALA A 304 20.569 30.258 25.480 1.00 40.66 A ATOM 1847 CB ALA A 304 20.121 30.004 24.040 1.00 41.36 A ATOM 1848 C ALA A 304 21.628 29.223 25.876 1.00 39.61 A ATOM 1849 O ALA A 304 21.298 28.156 26.395 1.00 40.61 A ATOM 1850 N PHE A 305 22.891 29.543 25.617 1.00 36.21 A ATOM 1851 CA PHE A 305 24.022 28.662 25.909 1.00 32.08 A ATOM 1852 CB PHE A 305 25.259 29.519 26.187 1.00 29.46 A ATOM 1853 CG PHE A 305 26.536 28.917 25.690 1.00 28.15 A ATOM 1854 CD1 PHE A 305 27.146 27.875 26.377 1.00 26.20 A ATOM 1855 CD2 PHE A 305 27.127 29.386 24.521 1.00 27.05 A ATOM 1856 CE1 PHE A 305 28.330 27.308 25.908 1.00 26.92 A ATOM 1857 CE2 PHE A 305 28.312 28.826 24.042 1.00 26.62 A ATOM 1858 CZ PHE A 305 28.914 27.786 24.737 1.00 26.61 A ATOM 1859 C PHE A 305 23.811 27.664 27.057 1.00 30.09 A ATOM 1860 O PHE A 305 23.518 28.051 28.187 1.00 31.51 A ATOM 1861 N PHE A 306 23.964 26.378 26.758 1.00 27.01 A ATOM 1862 CA PHE A 306 23.801 25.334 27.769 1.00 26.30 A ATOM 1863 CB PHE A 306 24.157 23.970 27.170 1.00 25.03 A ATOM 1864 CG PHE A 306 23.548 23.725 25.815 1.00 27.24 A ATOM 1865 CD1 PHE A 306 22.170 23.831 25.622 1.00 28.40 A ATOM 1866 CD2 PHE A 306 24.350 23.386 24.728 1.00 27.84 A ATOM 1867 CE1 PHE A 306 21.601 23.603 24.365 1.00 28.05 A ATOM 1868 CE2 PHE A 306 23.792 23.155 23.465 1.00 28.31 A ATOM 1869 CZ PHE A 306 22.415 23.263 23.283 1.00 28.00 A ATOM 1870 C PHE A 306 24.711 25.652 28.961 1.00 26.23 A ATOM 1871 O PHE A 306 25.927 25.775 28.811 1.00 25.59 A ATOM 1872 N PRO A 307 24.125 25.796 30.163 1.00 26.67 A ATOM 1873 CD PRO A 307 22.685 25.625 30.430 1.00 27.95 A ATOM 1874 CA PRO A 307 24.842 26.110 31.405 1.00 26.59 A ATOM 1875 CB PRO A 307 23.795 25.832 32.481 1.00 26.14 A ATOM 1876 CG PRO A 307 22.531 26.250 31.803 1.00 27.86 A ATOM 1877 C PRO A 307 26.145 25.355 31.659 1.00 25.58 A ATOM 1878 O PRO A 307 27.189 25.964 31.900 1.00 22.65 A ATOM 1879 N LYS A 308 26.085 24.031 31.620 1.00 24.46 A ATOM 1880 CA LYS A 308 27.274 23.232 31.867 1.00 23.91 A ATOM 1881 CB LYS A 308 26.887 21.760 32.024 1.00 23.25 A ATOM 1882 CG LYS A 308 26.062 21.532 33.285 1.00 28.49 A ATOM 1883 CD LYS A 308 25.618 20.093 33.466 1.00 30.17 A ATOM 1884 CE LYS A 308 24.760 19.973 34.722 1.00 33.12 A ATOM 1885 NZ LYS A 308 24.122 18.636 34.860 1.00 34.13 A ATOM 1886 C LYS A 308 28.314 23.426 30.769 1.00 22.84 A ATOM 1887 O LYS A 308 29.514 23.411 31.042 1.00 22.46 A ATOM 1888 N ALA A 309 27.861 23.621 29.534 1.00 21.59 A ATOM 1889 CA ALA A 309 28.792 23.848 28.432 1.00 20.02 A ATOM 1890 CB ALA A 309 28.056 23.856 27.106 1.00 18.80 A ATOM 1891 C ALA A 309 29.481 25.191 28.662 1.00 21.41 A ATOM 1892 O ALA A 309 30.680 25.335 28.427 1.00 21.39 A ATOM 1893 N ARG A 310 28.717 26.179 29.121 1.00 21.39 A ATOM 1894 CA ARG A 310 29.290 27.494 29.388 1.00 22.02 A ATOM 1895 CB ARG A 310 28.213 28.479 29.854 1.00 22.39 A ATOM 1896 CG ARG A 310 28.806 29.756 30.436 1.00 25.30 A ATOM 1897 CD ARG A 310 27.780 30.852 30.664 1.00 28.33 A ATOM 1898 NE ARG A 310 28.420 32.039 31.230 1.00 30.18 A ATOM 1899 CZ ARG A 310 27.901 33.263 31.203 1.00 32.07 A ATOM 1900 NH1 ARG A 310 26.719 33.477 30.634 1.00 31.19 A ATOM 1901 NH2 ARG A 310 28.567 34.277 31.742 1.00 30.49 A ATOM 1902 C ARG A 310 30.376 27.388 30.458 1.00 21.65 A ATOM 1903 O ARG A 310 31.464 27.949 30.311 1.00 20.36 A ATOM 1904 N ASP A 311 30.074 26.677 31.541 1.00 19.57 A ATOM 1905 CA ASP A 311 31.043 26.512 32.615 1.00 20.18 A ATOM 1906 CB ASP A 311 30.460 25.649 33.739 1.00 20.39 A ATOM 1907 CG ASP A 311 31.439 25.446 34.881 1.00 23.35 A ATOM 1908 OD1 ASP A 311 32.158 24.428 34.885 1.00 24.91 A ATOM 1909 OD2 ASP A 311 31.500 26.312 35.776 1.00 26.96 A ATOM 1910 C ASP A 311 32.322 25.877 32.073 1.00 19.73 A ATOM 1911 O ASP A 311 33.422 26.289 32.439 1.00 19.30 A ATOM 1912 N LEU A 312 32.179 24.891 31.188 1.00 16.32 A ATOM 1913 CA LEU A 312 33.349 24.226 30.611 1.00 16.66 A ATOM 1914 CB LEU A 312 32.927 23.035 29.744 1.00 16.12 A ATOM 1915 CG LEU A 312 34.050 22.320 28.974 1.00 14.73 A ATOM 1916 CD1 LEU A 312 35.192 21.935 29.912 1.00 14.56 A ATOM 1917 CD2 LEU A 312 33.477 21.084 28.289 1.00 14.22 A ATOM 1918 C LEU A 312 34.181 25.189 29.774 1.00 16.61 A ATOM 1919 O LEU A 312 35.402 25.241 29.910 1.00 16.20 A ATOM 1920 N VAL A 313 33.515 25.949 28.908 1.00 16.20 A ATOM 1921 CA VAL A 313 34.207 26.907 28.058 1.00 15.37 A ATOM 1922 CB VAL A 313 33.216 27.648 27.130 1.00 16.42 A ATOM 1923 CG1 VAL A 313 33.915 28.796 26.426 1.00 16.93 A ATOM 1924 CG2 VAL A 313 32.644 26.672 26.103 1.00 17.88 A ATOM 1925 C VAL A 313 34.960 27.923 28.911 1.00 17.39 A ATOM 1926 O VAL A 313 36.093 28.294 28.591 1.00 18.00 A ATOM 1927 N GLU A 314 34.342 28.364 30.004 1.00 17.61 A ATOM 1928 CA GLU A 314 34.986 29.331 30.885 1.00 20.43 A ATOM 1929 CB GLU A 314 34.009 29.816 31.959 1.00 22.14 A ATOM 1930 CG GLU A 314 32.800 30.550 31.396 1.00 26.52 A ATOM 1931 CD GLU A 314 31.852 31.025 32.478 1.00 31.26 A ATOM 1932 OE1 GLU A 314 31.580 30.246 33.417 1.00 33.48 A ATOM 1933 OE2 GLU A 314 31.370 32.173 32.387 1.00 34.81 A ATOM 1934 C GLU A 314 36.217 28.721 31.539 1.00 19.15 A ATOM 1935 O GLU A 314 37.134 29.433 31.934 1.00 21.47 A ATOM 1936 N LYS A 315 36.245 27.400 31.651 1.00 19.51 A ATOM 1937 CA LYS A 315 37.394 26.749 32.258 1.00 19.17 A ATOM 1938 CB LYS A 315 36.946 25.514 33.043 1.00 18.84 A ATOM 1939 CG LYS A 315 36.280 25.885 34.368 1.00 19.62 A ATOM 1940 CD LYS A 315 35.653 24.696 35.073 1.00 19.22 A ATOM 1941 CE LYS A 315 35.070 25.095 36.427 1.00 21.00 A ATOM 1942 NZ LYS A 315 36.119 25.552 37.381 1.00 19.53 A ATOM 1943 C LYS A 315 38.452 26.393 31.218 1.00 18.96 A ATOM 1944 O LYS A 315 39.511 25.873 31.561 1.00 19.85 A ATOM 1945 N LEU A 316 38.164 26.691 29.950 1.00 17.08 A ATOM 1946 CA LEU A 316 39.102 26.429 28.854 1.00 16.41 A ATOM 1947 CB LEU A 316 38.414 25.636 27.738 1.00 13.81 A ATOM 1948 CG LEU A 316 38.028 24.201 28.115 1.00 14.39 A ATOM 1949 CD1 LEU A 316 37.139 23.597 27.031 1.00 12.38 A ATOM 1950 CD2 LEU A 316 39.302 23.373 28.309 1.00 12.77 A ATOM 1951 C LEU A 316 39.652 27.743 28.290 1.00 17.12 A ATOM 1952 O LEU A 316 40.851 27.860 28.023 1.00 16.53 A ATOM 1953 N LEU A 317 38.780 28.729 28.105 1.00 16.27 A ATOM 1954 CA LEU A 317 39.228 30.022 27.596 1.00 17.52 A ATOM 1955 CB LEU A 317 38.083 30.752 26.887 1.00 16.37 A ATOM 1956 CG LEU A 317 37.448 29.973 25.727 1.00 18.81 A ATOM 1957 CD1 LEU A 317 36.415 30.851 25.018 1.00 16.47 A ATOM 1958 CD2 LEU A 317 38.528 29.526 24.741 1.00 17.87 A ATOM 1959 C LEU A 317 39.745 30.841 28.774 1.00 18.27 A ATOM 1960 O LEU A 317 39.078 31.753 29.273 1.00 18.58 A ATOM 1961 N VAL A 318 40.937 30.475 29.229 1.00 18.02 A ATOM 1962 CA VAL A 318 41.593 31.141 30.342 1.00 18.85 A ATOM 1963 CB VAL A 318 41.846 30.153 31.500 1.00 19.91 A ATOM 1964 CG1 VAL A 318 42.590 30.848 32.634 1.00 20.01 A ATOM 1965 CG2 VAL A 318 40.520 29.584 31.990 1.00 19.44 A ATOM 1966 C VAL A 318 42.923 31.657 29.811 1.00 19.67 A ATOM 1967 O VAL A 318 43.690 30.902 29.208 1.00 18.26 A ATOM 1968 N LEU A 319 43.197 32.939 30.028 1.00 20.07 A ATOM 1969 CA LEU A 319 44.436 33.533 29.538 1.00 20.98 A ATOM 1970 CB LEU A 319 44.521 35.002 29.968 1.00 21.64 A ATOM 1971 CG LEU A 319 43.418 35.908 29.408 1.00 24.38 A ATOM 1972 CD1 LEU A 319 43.606 37.332 29.935 1.00 23.28 A ATOM 1973 CD2 LEU A 319 43.453 35.887 27.875 1.00 24.33 A ATOM 1974 C LEU A 319 45.680 32.774 29.994 1.00 20.38 A ATOM 1975 O LEU A 319 46.568 32.496 29.192 1.00 21.34 A ATOM 1976 N ASP A 320 45.742 32.440 31.280 1.00 20.22 A ATOM 1977 CA ASP A 320 46.879 31.707 31.833 1.00 20.90 A ATOM 1978 CB ASP A 320 46.842 31.760 33.365 1.00 20.76 A ATOM 1979 CG ASP A 320 48.049 31.102 34.004 1.00 21.51 A ATOM 1980 OD1 ASP A 320 48.669 30.226 33.367 1.00 23.46 A ATOM 1981 OD2 ASP A 320 48.371 31.450 35.159 1.00 23.89 A ATOM 1982 C ASP A 320 46.814 30.247 31.367 1.00 20.06 A ATOM 1983 O ASP A 320 45.988 29.476 31.840 1.00 20.54 A ATOM 1984 N ALA A 321 47.700 29.876 30.451 1.00 20.68 A ATOM 1985 CA ALA A 321 47.733 28.522 29.903 1.00 22.04 A ATOM 1986 CB ALA A 321 48.860 28.411 28.881 1.00 20.75 A ATOM 1987 C ALA A 321 47.858 27.400 30.940 1.00 21.62 A ATOM 1988 O ALA A 321 47.482 26.259 30.665 1.00 21.99 A ATOM 1989 N THR A 322 48.372 27.715 32.127 1.00 20.89 A ATOM 1990 CA THR A 322 48.531 26.698 33.167 1.00 20.82 A ATOM 1991 CB THR A 322 49.670 27.051 34.146 1.00 19.47 A ATOM 1992 OG1 THR A 322 49.341 28.253 34.848 1.00 20.19 A ATOM 1993 CG2 THR A 322 50.981 27.249 33.394 1.00 21.59 A ATOM 1994 C THR A 322 47.264 26.498 33.983 1.00 19.55 A ATOM 1995 O THR A 322 47.235 25.673 34.894 1.00 21.13 A ATOM 1996 N LYS A 323 46.216 27.248 33.661 1.00 19.33 A ATOM 1997 CA LYS A 323 44.962 27.122 34.392 1.00 21.20 A ATOM 1998 CB LYS A 323 44.580 28.460 35.030 1.00 23.75 A ATOM 1999 CG LYS A 323 45.562 28.933 36.084 1.00 28.45 A ATOM 2000 CD LYS A 323 45.055 30.177 36.799 1.00 33.76 A ATOM 2001 CE LYS A 323 46.087 30.678 37.802 1.00 36.15 A ATOM 2002 NZ LYS A 323 46.532 29.569 38.693 1.00 37.34 A ATOM 2003 C LYS A 323 43.806 26.614 33.539 1.00 20.68 A ATOM 2004 O LYS A 323 42.649 26.757 33.915 1.00 20.42 A ATOM 2005 N ARG A 324 44.114 26.019 32.392 1.00 19.97 A ATOM 2006 CA ARG A 324 43.060 25.494 31.531 1.00 17.98 A ATOM 2007 CB ARG A 324 43.461 25.609 30.061 1.00 15.95 A ATOM 2008 CG ARG A 324 43.534 27.050 29.603 1.00 17.34 A ATOM 2009 CD ARG A 324 43.996 27.194 28.172 1.00 19.80 A ATOM 2010 NE ARG A 324 44.438 28.565 27.944 1.00 16.93 A ATOM 2011 CZ ARG A 324 45.410 28.908 27.108 1.00 19.88 A ATOM 2012 NH1 ARG A 324 46.045 27.978 26.398 1.00 14.58 A ATOM 2013 NH2 ARG A 324 45.774 30.181 27.015 1.00 16.51 A ATOM 2014 C ARG A 324 42.762 24.046 31.883 1.00 18.32 A ATOM 2015 O ARG A 324 43.673 23.222 32.006 1.00 18.20 A ATOM 2016 N LEU A 325 41.479 23.748 32.055 1.00 18.32 A ATOM 2017 CA LEU A 325 41.050 22.403 32.395 1.00 17.79 A ATOM 2018 CB LEU A 325 39.523 22.335 32.425 1.00 17.03 A ATOM 2019 CG LEU A 325 38.896 21.125 33.116 1.00 15.91 A ATOM 2020 CD1 LEU A 325 39.392 21.048 34.557 1.00 15.93 A ATOM 2021 CD2 LEU A 325 37.375 21.255 33.084 1.00 16.56 A ATOM 2022 C LEU A 325 41.599 21.433 31.356 1.00 18.68 A ATOM 2023 O LEU A 325 41.347 21.586 30.157 1.00 18.28 A ATOM 2024 N GLY A 326 42.354 20.439 31.821 1.00 18.18 A ATOM 2025 CA GLY A 326 42.931 19.462 30.915 1.00 16.36 A ATOM 2026 C GLY A 326 44.443 19.558 30.807 1.00 19.15 A ATOM 2027 O GLY A 326 45.093 18.592 30.404 1.00 19.52 A ATOM 2028 N CYS A 327 45.016 20.708 31.161 1.00 18.16 A ATOM 2029 CA CYS A 327 46.463 20.867 31.075 1.00 19.30 A ATOM 2030 CB CYS A 327 46.856 22.350 31.058 1.00 20.22 A ATOM 2031 SG CYS A 327 46.782 23.200 32.649 1.00 21.97 A ATOM 2032 C CYS A 327 47.169 20.157 32.228 1.00 20.22 A ATOM 2033 O CYS A 327 46.561 19.828 33.246 1.00 17.92 A ATOM 2034 N GLU A 328 48.463 19.933 32.053 1.00 20.51 A ATOM 2035 CA GLU A 328 49.274 19.244 33.042 1.00 23.34 A ATOM 2036 CB GLU A 328 50.710 19.139 32.507 1.00 28.68 A ATOM 2037 CG GLU A 328 50.754 18.367 31.175 1.00 38.24 A ATOM 2038 CD GLU A 328 52.067 18.500 30.414 1.00 43.23 A ATOM 2039 OE1 GLU A 328 52.535 19.643 30.218 1.00 46.22 A ATOM 2040 OE2 GLU A 328 52.618 17.459 29.991 1.00 44.90 A ATOM 2041 C GLU A 328 49.234 19.876 34.435 1.00 22.11 A ATOM 2042 O GLU A 328 49.147 19.161 35.437 1.00 20.27 A ATOM 2043 N GLU A 329 49.276 21.204 34.506 1.00 18.40 A ATOM 2044 CA GLU A 329 49.248 21.875 35.801 1.00 20.13 A ATOM 2045 CB GLU A 329 49.587 23.363 35.657 1.00 20.36 A ATOM 2046 CG GLU A 329 51.014 23.651 35.190 1.00 24.05 A ATOM 2047 CD GLU A 329 51.191 23.518 33.688 1.00 25.93 A ATOM 2048 OE1 GLU A 329 50.213 23.154 32.995 1.00 26.61 A ATOM 2049 OE2 GLU A 329 52.311 23.781 33.198 1.00 27.19 A ATOM 2050 C GLU A 329 47.890 21.718 36.480 1.00 19.36 A ATOM 2051 O GLU A 329 47.775 21.879 37.694 1.00 18.74 A ATOM 2052 N MET A 330 46.863 21.415 35.691 1.00 17.28 A ATOM 2053 CA MET A 330 45.520 21.220 36.229 1.00 16.38 A ATOM 2054 CB MET A 330 44.474 21.833 35.294 1.00 17.65 A ATOM 2055 CG MET A 330 44.460 23.365 35.311 1.00 22.95 A ATOM 2056 SD MET A 330 44.186 24.026 36.979 1.00 26.78 A ATOM 2057 CZ MET A 330 42.435 23.712 37.186 1.00 24.69 A ATOM 2058 C MET A 330 45.257 19.730 36.422 1.00 14.30 A ATOM 2059 O MET A 330 44.127 19.304 36.629 1.00 15.39 A ATOM 2060 N GLU A 331 46.327 18.949 36.346 1.00 15.60 A ATOM 2061 CA GLU A 331 46.289 17.501 36.531 1.00 17.08 A ATOM 2062 CB GLU A 331 45.607 17.155 37.862 1.00 17.00 A ATOM 2063 CG GLU A 331 46.070 18.027 39.038 1.00 17.46 A ATOM 2064 CD GLU A 331 47.591 18.179 39.145 1.00 20.16 A ATOM 2065 OE1 GLU A 331 48.034 19.073 39.896 1.00 21.39 A ATOM 2066 OE2 GLU A 331 48.345 17.420 38.500 1.00 18.87 A ATOM 2067 C GLU A 331 45.697 16.658 35.398 1.00 17.80 A ATOM 2068 O GLU A 331 45.107 15.602 35.636 1.00 20.40 A ATOM 2069 N GLY A 332 45.844 17.133 34.167 1.00 16.23 A ATOM 2070 CA GLY A 332 45.420 16.353 33.015 1.00 14.10 A ATOM 2071 C GLY A 332 43.982 16.154 32.596 1.00 13.54 A ATOM 2072 O GLY A 332 43.063 16.864 33.017 1.00 11.96 A ATOM 2073 N TYR A 333 43.804 15.141 31.750 1.00 14.37 A ATOM 2074 CA TYR A 333 42.510 14.806 31.182 1.00 13.56 A ATOM 2075 CB TYR A 333 42.722 13.892 29.968 1.00 15.00 A ATOM 2076 CG TYR A 333 43.153 14.683 28.752 1.00 16.46 A ATOM 2077 CD1 TYR A 333 42.206 15.172 27.849 1.00 15.29 A ATOM 2078 CE1 TYR A 333 42.573 16.002 26.794 1.00 13.42 A ATOM 2079 CD2 TYR A 333 44.490 15.039 28.561 1.00 14.91 A ATOM 2080 CE2 TYR A 333 44.872 15.877 27.499 1.00 14.87 A ATOM 2081 CZ TYR A 333 43.902 16.353 26.626 1.00 15.61 A ATOM 2082 OH TYR A 333 44.244 17.197 25.599 1.00 17.29 A ATOM 2083 C TYR A 333 41.470 14.230 32.127 1.00 15.23 A ATOM 2084 O TYR A 333 40.278 14.323 31.846 1.00 16.63 A ATOM 2085 N GLY A 334 41.907 13.650 33.244 1.00 15.50 A ATOM 2086 CA GLY A 334 40.957 13.100 34.202 1.00 15.07 A ATOM 2087 C GLY A 334 39.925 14.146 34.616 1.00 16.40 A ATOM 2088 O GLY A 334 38.724 13.946 34.433 1.00 15.05 A ATOM 2089 N PRO A 335 40.366 15.278 35.184 1.00 14.96 A ATOM 2090 CD PRO A 335 41.727 15.531 35.689 1.00 15.88 A ATOM 2091 CA PRO A 335 39.444 16.339 35.606 1.00 15.29 A ATOM 2092 CB PRO A 335 40.383 17.397 36.178 1.00 13.19 A ATOM 2093 CG PRO A 335 41.485 16.569 36.758 1.00 13.81 A ATOM 2094 C PRO A 335 38.594 16.877 34.448 1.00 15.84 A ATOM 2095 O PRO A 335 37.423 17.204 34.631 1.00 14.84 A ATOM 2096 N LEU A 336 39.184 16.971 33.257 1.00 16.12 A ATOM 2097 CA LEU A 336 38.450 17.465 32.094 1.00 15.52 A ATOM 2098 CB LEU A 336 39.396 17.653 30.898 1.00 14.39 A ATOM 2099 CG LEU A 336 38.770 17.991 29.538 1.00 15.46 A ATOM 2100 CD1 LEU A 336 37.836 19.182 29.662 1.00 11.25 A ATOM 2101 CD2 LEU A 336 39.884 18.285 28.528 1.00 14.11 A ATOM 2102 C LEU A 336 37.321 16.508 31.714 1.00 16.28 A ATOM 2103 O LEU A 336 36.176 16.921 31.540 1.00 15.51 A ATOM 2104 N LYS A 337 37.640 15.225 31.592 1.00 17.22 A ATOM 2105 CA LYS A 337 36.624 14.243 31.235 1.00 17.39 A ATOM 2106 CB LYS A 337 37.293 12.900 30.921 1.00 17.68 A ATOM 2107 CG LYS A 337 38.170 12.994 29.676 1.00 22.31 A ATOM 2108 CD LYS A 337 39.213 11.892 29.592 1.00 24.60 A ATOM 2109 CE LYS A 337 38.620 10.560 29.189 1.00 24.76 A ATOM 2110 NZ LYS A 337 39.710 9.560 28.997 1.00 25.05 A ATOM 2111 C LYS A 337 35.577 14.096 32.342 1.00 17.33 A ATOM 2112 O LYS A 337 34.456 13.652 32.090 1.00 14.42 A ATOM 2113 N ALA A 338 35.928 14.500 33.559 1.00 15.83 A ATOM 2114 CA ALA A 338 34.989 14.395 34.674 1.00 17.52 A ATOM 2115 CB ALA A 338 35.749 14.167 35.980 1.00 19.68 A ATOM 2116 C ALA A 338 34.095 15.621 34.804 1.00 18.83 A ATOM 2117 O ALA A 338 33.252 15.687 35.695 1.00 18.94 A ATOM 2118 N HIS A 339 34.262 16.596 33.918 1.00 19.42 A ATOM 2119 CA HIS A 339 33.438 17.796 34.004 1.00 19.28 A ATOM 2120 CB HIS A 339 33.865 18.819 32.949 1.00 19.20 A ATOM 2121 CG HIS A 339 33.163 20.134 33.074 1.00 20.26 A ATOM 2122 CD2 HIS A 339 33.549 21.299 33.649 1.00 18.95 A ATOM 2123 ND1 HIS A 339 31.880 20.340 32.612 1.00 19.10 A ATOM 2124 CE1 HIS A 339 31.506 21.576 32.896 1.00 22.19 A ATOM 2125 NE2 HIS A 339 32.500 22.179 33.525 1.00 21.98 A ATOM 2126 C HIS A 339 31.957 17.448 33.845 1.00 19.13 A ATOM 2127 O HIS A 339 31.597 16.576 33.061 1.00 19.52 A ATOM 2128 N PRO A 340 31.079 18.125 34.606 1.00 19.80 A ATOM 2129 CD PRO A 340 31.424 19.119 35.640 1.00 19.08 A ATOM 2130 CA PRO A 340 29.630 17.900 34.569 1.00 20.52 A ATOM 2131 CB PRO A 340 29.091 19.058 35.396 1.00 20.74 A ATOM 2132 CG PRO A 340 30.146 19.207 36.454 1.00 19.20 A ATOM 2133 C PRO A 340 29.000 17.834 33.176 1.00 21.42 A ATOM 2134 O PRO A 340 28.049 17.088 32.955 1.00 22.48 A ATOM 2135 N PHE A 341 29.528 18.606 32.237 1.00 21.33 A ATOM 2136 CA PHE A 341 28.985 18.610 30.886 1.00 21.57 A ATOM 2137 CB PHE A 341 29.739 19.624 30.017 1.00 21.64 A ATOM 2138 CG PHE A 341 29.207 19.740 28.613 1.00 23.18 A ATOM 2139 CD1 PHE A 341 27.903 20.171 28.382 1.00 22.58 A ATOM 2140 CD2 PHE A 341 30.013 19.431 27.522 1.00 21.95 A ATOM 2141 CE1 PHE A 341 27.410 20.292 27.082 1.00 23.54 A ATOM 2142 CE2 PHE A 341 29.533 19.548 26.220 1.00 21.83 A ATOM 2143 CZ PHE A 341 28.228 19.980 25.998 1.00 23.23 A ATOM 2144 C PHE A 341 29.055 17.226 30.237 1.00 21.84 A ATOM 2145 O PHE A 341 28.232 16.896 29.389 1.00 20.37 A ATOM 2146 N PHE A 342 30.034 16.422 30.640 1.00 20.51 A ATOM 2147 CA PHE A 342 30.221 15.085 30.077 1.00 23.01 A ATOM 2148 CB PHE A 342 31.710 14.809 29.850 1.00 18.00 A ATOM 2149 CG PHE A 342 32.398 15.812 28.971 1.00 17.05 A ATOM 2150 CD1 PHE A 342 32.010 15.987 27.652 1.00 17.78 A ATOM 2151 CD2 PHE A 342 33.487 16.534 29.450 1.00 15.72 A ATOM 2152 CE1 PHE A 342 32.702 16.867 26.811 1.00 18.08 A ATOM 2153 CE2 PHE A 342 34.184 17.414 28.617 1.00 17.45 A ATOM 2154 CZ PHE A 342 33.790 17.578 27.298 1.00 16.56 A ATOM 2155 C PHE A 342 29.679 13.972 30.976 1.00 24.95 A ATOM 2156 O PHE A 342 30.002 12.798 30.777 1.00 23.95 A ATOM 2157 N GLU A 343 28.861 14.333 31.958 1.00 27.35 A ATOM 2158 CA GLU A 343 28.325 13.349 32.897 1.00 30.28 A ATOM 2159 CB GLU A 343 27.187 13.964 33.716 1.00 32.20 A ATOM 2160 CG GLU A 343 26.581 12.991 34.714 1.00 39.71 A ATOM 2161 CD GLU A 343 25.628 13.661 35.688 1.00 44.72 A ATOM 2162 OE1 GLU A 343 24.661 14.314 35.234 1.00 47.55 A ATOM 2163 OE2 GLU A 343 25.847 13.526 36.911 1.00 46.89 A ATOM 2164 C GLU A 343 27.852 12.017 32.305 1.00 28.98 A ATOM 2165 O GLU A 343 28.225 10.952 32.800 1.00 31.73 A ATOM 2166 N SER A 344 27.037 12.067 31.258 1.00 26.09 A ATOM 2167 CA SER A 344 26.520 10.838 30.656 1.00 28.36 A ATOM 2168 CB SER A 344 25.129 11.089 30.067 1.00 28.73 A ATOM 2169 OG SER A 344 25.203 11.942 28.940 1.00 30.91 A ATOM 2170 C SER A 344 27.407 10.214 29.577 1.00 27.66 A ATOM 2171 O SER A 344 26.987 9.281 28.900 1.00 28.66 A ATOM 2172 N VAL A 345 28.627 10.715 29.419 1.00 26.75 A ATOM 2173 CA VAL A 345 29.534 10.183 28.402 1.00 23.44 A ATOM 2174 CB VAL A 345 30.565 11.256 27.950 1.00 23.10 A ATOM 2175 CG1 VAL A 345 31.589 10.631 26.995 1.00 22.24 A ATOM 2176 CG2 VAL A 345 29.854 12.418 27.275 1.00 20.05 A ATOM 2177 C VAL A 345 30.326 8.957 28.855 1.00 24.26 A ATOM 2178 O VAL A 345 30.876 8.930 29.960 1.00 22.83 A ATOM 2179 N THR A 346 30.374 7.942 27.997 1.00 21.77 A ATOM 2180 CA THR A 346 31.153 6.740 28.272 1.00 23.70 A ATOM 2181 CB THR A 346 30.391 5.455 27.857 1.00 26.53 A ATOM 2182 OG1 THR A 346 29.248 5.284 28.706 1.00 29.98 A ATOM 2183 CG2 THR A 346 31.289 4.231 27.990 1.00 24.28 A ATOM 2184 C THR A 346 32.383 6.945 27.385 1.00 23.43 A ATOM 2185 O THR A 346 32.306 6.827 26.160 1.00 24.50 A ATOM 2186 N TRP A 347 33.508 7.270 28.013 1.00 22.98 A ATOM 2187 CA TRP A 347 34.744 7.569 27.300 1.00 23.81 A ATOM 2188 CB TRP A 347 35.683 8.352 28.219 1.00 22.54 A ATOM 2189 CG TRP A 347 35.128 9.658 28.693 1.00 20.61 A ATOM 2190 CD2 TRP A 347 35.257 10.927 28.040 1.00 19.11 A ATOM 2191 CE2 TRP A 347 34.581 11.881 28.838 1.00 18.39 A ATOM 2192 CE3 TRP A 347 35.878 11.351 26.858 1.00 18.16 A ATOM 2193 CD1 TRP A 347 34.397 9.883 29.828 1.00 18.35 A ATOM 2194 NE1 TRP A 347 34.065 11.218 29.923 1.00 19.51 A ATOM 2195 CZ2 TRP A 347 34.510 13.234 28.491 1.00 16.88 A ATOM 2196 CZ3 TRP A 347 35.808 12.701 26.511 1.00 17.23 A ATOM 2197 CH2 TRP A 347 35.127 13.624 27.327 1.00 18.16 A ATOM 2198 C TRP A 347 35.538 6.429 26.675 1.00 25.79 A ATOM 2199 O TRP A 347 36.304 6.654 25.742 1.00 24.67 A ATOM 2200 N ALA A 348 35.360 5.215 27.183 1.00 27.10 A ATOM 2201 CA ALA A 348 36.116 4.063 26.697 1.00 27.46 A ATOM 2202 CB ALA A 348 35.899 2.869 27.636 1.00 27.09 A ATOM 2203 C ALA A 348 35.895 3.620 25.256 1.00 27.18 A ATOM 2204 O ALA A 348 36.830 3.148 24.613 1.00 29.41 A ATOM 2205 N ASN A 349 34.682 3.769 24.735 1.00 26.55 A ATOM 2206 CA ASN A 349 34.418 3.310 23.375 1.00 27.28 A ATOM 2207 CB ASN A 349 33.700 1.962 23.444 1.00 29.37 A ATOM 2208 CG ASN A 349 32.299 2.088 24.013 1.00 30.92 A ATOM 2209 OD1 ASN A 349 32.045 2.942 24.859 1.00 30.17 A ATOM 2210 ND2 ASN A 349 31.386 1.237 23.553 1.00 33.52 A ATOM 2211 C ASN A 349 33.599 4.265 22.509 1.00 26.47 A ATOM 2212 O ASN A 349 32.669 3.843 21.819 1.00 25.87 A ATOM 2213 N LEU A 350 33.947 5.543 22.518 1.00 24.45 A ATOM 2214 CA LEU A 350 33.203 6.510 21.721 1.00 23.14 A ATOM 2215 CB LEU A 350 33.837 7.898 21.848 1.00 23.22 A ATOM 2216 CG LEU A 350 33.659 8.605 23.191 1.00 21.05 A ATOM 2217 CD1 LEU A 350 34.646 9.756 23.293 1.00 19.36 A ATOM 2218 CD2 LEU A 350 32.220 9.094 23.319 1.00 18.78 A ATOM 2219 C LEU A 350 33.082 6.152 20.240 1.00 22.60 A ATOM 2220 O LEU A 350 32.011 6.296 19.650 1.00 21.15 A ATOM 2221 N HIS A 351 34.165 5.689 19.627 1.00 23.13 A ATOM 2222 CA HIS A 351 34.089 5.387 18.204 1.00 27.83 A ATOM 2223 CB HIS A 351 35.506 5.325 17.596 1.00 29.36 A ATOM 2224 CG HIS A 351 36.082 3.950 17.493 1.00 32.07 A ATOM 2225 CD2 HIS A 351 36.611 3.128 18.431 1.00 32.39 A ATOM 2226 ND1 HIS A 351 36.197 3.285 16.291 1.00 33.02 A ATOM 2227 CE1 HIS A 351 36.775 2.113 16.493 1.00 33.58 A ATOM 2228 NE2 HIS A 351 37.036 1.992 17.782 1.00 31.76 A ATOM 2229 C HIS A 351 33.258 4.144 17.874 1.00 28.12 A ATOM 2230 O HIS A 351 33.015 3.847 16.707 1.00 29.49 A ATOM 2231 N GLN A 352 32.800 3.442 18.908 1.00 29.28 A ATOM 2232 CA GLN A 352 31.963 2.255 18.726 1.00 29.67 A ATOM 2233 CB GLN A 352 32.366 1.145 19.694 1.00 30.56 A ATOM 2234 CG GLN A 352 33.169 0.041 19.041 1.00 30.88 A ATOM 2235 CD GLN A 352 34.493 −0.186 19.729 1.00 31.21 A ATOM 2236 OE1 GLN A 352 34.541 −0.450 20.928 1.00 30.76 A ATOM 2237 NE2 GLN A 352 35.578 −0.084 18.971 1.00 32.30 A ATOM 2238 C GLN A 352 30.504 2.638 18.963 1.00 30.42 A ATOM 2239 O GLN A 352 29.595 1.831 18.770 1.00 29.01 A ATOM 2240 N GLN A 353 30.290 3.875 19.397 1.00 27.64 A ATOM 2241 CA GLN A 353 28.948 4.365 19.652 1.00 27.42 A ATOM 2242 CB GLN A 353 28.977 5.401 20.775 1.00 25.77 A ATOM 2243 CG GLN A 353 29.408 4.837 22.115 1.00 27.34 A ATOM 2244 CD GLN A 353 29.638 5.914 23.156 1.00 27.19 A ATOM 2245 OE1 GLN A 353 28.875 6.872 23.252 1.00 28.29 A ATOM 2246 NE2 GLN A 353 30.687 5.753 23.951 1.00 28.79 A ATOM 2247 C GLN A 353 28.375 4.989 18.385 1.00 29.00 A ATOM 2248 O GLN A 353 29.118 5.455 17.516 1.00 29.14 A ATOM 2249 N THR A 354 27.053 4.984 18.276 1.00 27.31 A ATOM 2250 CA THR A 354 26.390 5.568 17.119 1.00 27.85 A ATOM 2251 CB THR A 354 24.991 4.941 16.904 1.00 30.69 A ATOM 2252 OG1 THR A 354 25.132 3.532 16.665 1.00 30.07 A ATOM 2253 CG2 THR A 354 24.289 5.585 15.709 1.00 29.58 A ATOM 2254 C THR A 354 26.244 7.062 17.376 1.00 26.85 A ATOM 2255 O THR A 354 25.592 7.475 18.329 1.00 25.77 A ATOM 2256 N PRO A 355 26.867 7.898 16.533 1.00 27.22 A ATOM 2257 CD PRO A 355 27.792 7.588 15.431 1.00 25.89 A ATOM 2258 CA PRO A 355 26.763 9.346 16.734 1.00 27.23 A ATOM 2259 CB PRO A 355 27.625 9.915 15.609 1.00 24.91 A ATOM 2260 CG PRO A 355 28.643 8.838 15.385 1.00 25.54 A ATOM 2261 C PRO A 355 25.322 9.837 16.641 1.00 28.07 A ATOM 2262 O PRO A 355 24.548 9.364 15.810 1.00 27.24 A ATOM 2263 N PRO A 356 24.941 10.792 17.500 1.00 28.28 A ATOM 2264 CD PRO A 356 25.752 11.560 18.462 1.00 28.31 A ATOM 2265 CA PRO A 356 23.572 11.306 17.448 1.00 28.44 A ATOM 2266 CB PRO A 356 23.539 12.301 18.604 1.00 28.11 A ATOM 2267 CG PRO A 356 24.946 12.832 18.612 1.00 26.86 A ATOM 2268 C PRO A 356 23.363 11.978 16.097 1.00 29.25 A ATOM 2269 O PRO A 356 24.304 12.537 15.529 1.00 27.27 A ATOM 2270 N ALA A 357 22.143 11.910 15.575 1.00 30.45 A ATOM 2271 CA ALA A 357 21.848 12.521 14.287 1.00 32.81 A ATOM 2272 CB ALA A 357 20.507 12.019 13.757 1.00 31.99 A ATOM 2273 C ALA A 357 21.824 14.035 14.448 1.00 35.05 A ATOM 2274 O ALA A 357 21.194 14.561 15.369 1.00 35.04 A ATOM 2275 N LEU A 358 22.516 14.730 13.552 1.00 37.81 A ATOM 2276 CA LEU A 358 22.578 16.185 13.597 1.00 42.15 A ATOM 2277 CB LEU A 358 23.679 16.681 12.658 1.00 39.54 A ATOM 2278 CG LEU A 358 25.086 16.285 13.109 1.00 39.51 A ATOM 2279 CD1 LEU A 358 26.102 16.686 12.062 1.00 39.29 A ATOM 2280 CD2 LEU A 358 25.395 16.953 14.445 1.00 40.01 A ATOM 2281 C LEU A 358 21.241 16.837 13.242 1.00 45.91 A ATOM 2282 O LEU A 358 20.874 16.927 12.069 1.00 45.71 A ATOM 2283 N THR A 359 20.530 17.290 14.275 1.00 50.06 A ATOM 2284 CA THR A 359 19.223 17.939 14.140 1.00 53.73 A ATOM 2285 CB THR A 359 19.353 19.428 13.726 1.00 54.04 A ATOM 2286 OG1 THR A 359 19.995 19.521 12.448 1.00 56.35 A ATOM 2287 CG2 THR A 359 20.158 20.204 14.763 1.00 54.32 A ATOM 2288 C THR A 359 18.309 17.236 13.139 1.00 54.47 A ATOM 2289 O THR A 359 18.483 16.016 12.930 1.00 55.90 A ATOM 2290 OXT THR A 359 17.407 17.908 12.595 1.00 56.97 A TER ATOM 1 CB PRO B 71 99.838 54.646 −7.659 1.00 20.00 6 ATOM 2 CG PRO B 71 99.216 55.105 −6.341 1.00 20.00 6 ATOM 3 C PRO B 71 98.903 54.776 −9.981 1.00 20.00 6 ATOM 4 O PRO B 71 98.022 53.925 −10.109 1.00 20.00 8 ATOM 5 N PRO B 71 97.782 55.851 −8.042 1.00 20.00 7 ATOM 6 CD PRO B 71 97.728 55.323 −6.668 1.00 20.00 6 ATOM 7 CA PRO B 71 99.087 55.515 −8.658 1.00 20.00 6 ATOM 8 N PRO B 72 99.732 55.097 −10.985 1.00 20.00 7 ATOM 9 CD PRO B 72 100.794 56.121 −10.977 1.00 20.00 6 ATOM 10 CA PRO B 72 99.645 54.451 −12.297 1.00 20.00 6 ATOM 11 CB PRO B 72 100.885 54.973 −13.017 1.00 20.00 6 ATOM 12 CG PRO B 72 101.026 56.352 −12.456 1.00 20.00 6 ATOM 13 C PRO B 72 99.627 52.924 −12.202 1.00 20.00 6 ATOM 14 O PRO B 72 100.246 52.338 −11.314 1.00 20.00 8 ATOM 15 N ALA B 73 98.906 52.293 −13.122 1.00 20.00 7 ATOM 16 CA ALA B 73 98.805 50.840 −13.167 1.00 20.00 6 ATOM 17 CB ALA B 73 97.420 50.392 −12.710 1.00 20.00 6 ATOM 18 C ALA B 73 99.053 50.398 −14.604 1.00 20.00 6 ATOM 19 O ALA B 73 99.027 51.215 −15.526 1.00 20.00 8 ATOM 20 N PRO B 74 99.313 49.100 −14.818 1.00 20.00 7 ATOM 21 CD PRO B 74 99.473 47.995 −13.857 1.00 20.00 6 ATOM 22 CA PRO B 74 99.553 48.642 −16.189 1.00 20.00 6 ATOM 23 CB PRO B 74 99.700 47.132 −16.023 1.00 20.00 6 ATOM 24 CG PRO B 74 100.292 47.004 −14.649 1.00 20.00 6 ATOM 25 C PRO B 74 98.371 49.018 −17.079 1.00 20.00 6 ATOM 26 O PRO B 74 97.279 49.296 −16.583 1.00 20.00 8 ATOM 27 N ALA B 75 98.589 49.037 −18.389 1.00 20.00 7 ATOM 28 CA ALA B 75 97.516 49.368 −19.321 1.00 20.00 6 ATOM 29 CB ALA B 75 98.061 49.462 −20.745 1.00 20.00 6 ATOM 30 C ALA B 75 96.446 48.285 −19.246 1.00 20.00 6 ATOM 31 O ALA B 75 96.745 47.126 −18.961 1.00 20.00 8 ATOM 32 N LYS B 76 95.200 48.666 −19.494 1.00 20.00 7 ATOM 33 CA LYS B 76 94.098 47.716 −19.463 1.00 20.00 6 ATOM 34 CB LYS B 76 92.793 48.431 −19.805 1.00 20.00 6 ATOM 35 CG LYS B 76 91.546 47.792 −19.225 1.00 20.00 6 ATOM 36 CD LYS B 76 91.511 47.932 −17.711 1.00 20.00 6 ATOM 37 CZ LYS B 76 90.184 47.454 −17.152 1.00 20.00 6 ATOM 38 NZ LYS B 76 90.108 47.606 −15.673 1.00 20.00 7 ATOM 39 C LYS B 76 94.389 46.645 −20.513 1.00 20.00 6 ATOM 40 O LYS B 76 94.736 46.968 −21.645 1.00 20.00 8 ATOM 41 N LYS B 77 94.269 45.374 −20.145 1.00 20.00 7 ATOM 42 CA LYS B 77 94.525 44.311 −21.107 1.00 20.00 6 ATOM 43 CB LYS B 77 94.875 43.008 −20.384 1.00 20.00 6 ATOM 44 CG LYS B 77 96.117 43.125 −19.506 1.00 20.00 6 ATOM 45 CD LYS B 77 96.461 41.812 −18.842 1.00 20.00 6 ATOM 46 CE LYS B 77 97.501 42.008 −17.745 1.00 20.00 6 ATOM 47 NZ LYS B 77 98.771 42.582 −18.255 1.00 20.00 7 ATOM 48 C LYS B 77 93.311 44.111 −22.012 1.00 20.00 6 ATOM 49 O LYS B 77 92.218 44.585 −21.704 1.00 20.00 8 ATOM 50 N ARG B 78 93.514 43.418 −23.129 1.00 20.00 7 ATOM 51 CA ARG B 78 92.442 43.158 −24.086 1.00 20.00 6 ATOM 52 CB ARG B 78 92.465 44.224 −25.193 1.00 20.00 6 ATOM 53 CG ARG B 78 93.787 44.344 −25.925 1.00 20.00 6 ATOM 54 CD ARG B 78 93.833 45.612 −26.771 1.00 20.00 6 ATOM 55 NE ARG B 78 95.052 45.702 −27.575 1.00 20.00 7 ATOM 56 CZ ARG B 78 96.287 45.751 −27.078 1.00 20.00 6 ATOM 57 NH1 ARG B 78 96.486 45.721 −25.764 1.00 20.00 7 ATOM 58 NH2 ARG B 78 97.330 45.828 −27.897 1.00 20.00 7 ATOM 59 C ARG B 78 92.570 41.754 −24.678 1.00 20.00 6 ATOM 60 O ARG B 78 93.625 41.126 −24.581 1.00 20.00 8 ATOM 61 N PRO B 79 91.494 41.240 −25.303 1.00 20.00 7 ATOM 62 CD PRO B 79 90.195 41.894 −25.543 1.00 20.00 6 ATOM 63 CA PRO B 79 91.519 39.899 −25.896 1.00 20.00 6 ATOM 64 CB PRO B 79 90.214 39.848 −26.691 1.00 20.00 6 ATOM 65 CG PRO B 79 89.304 40.725 −25.889 1.00 20.00 6 ATOM 66 C PRO B 79 92.737 39.614 −26.778 1.00 20.00 6 ATOM 67 O PRO B 79 93.311 38.523 −26.717 1.00 20.00 8 ATOM 68 N GLU B 80 93.124 40.597 −27.589 1.00 20.00 7 ATOM 69 CA GLU B 80 94.254 40.441 −28.503 1.00 20.00 6 ATOM 70 CB GLU B 80 94.358 41.644 −29.446 1.00 20.00 6 ATOM 71 CG GLU B 80 94.881 42.912 −28.800 1.00 20.00 6 ATOM 72 CD GLU B 80 95.009 44.057 −29.788 1.00 20.00 6 ATOM 73 OE1 GLU B 80 93.968 44.513 −30.308 1.00 20.00 8 ATOM 74 OE2 GLU B 80 96.150 44.498 −30.047 1.00 20.00 8 ATOM 75 C GLU B 80 95.591 40.235 −27.787 1.00 20.00 6 ATOM 76 O GLU B 80 96.558 39.795 −28.405 1.00 20.00 8 ATOM 77 N ASP B 81 95.656 40.559 −26.497 1.00 20.00 7 ATOM 78 CA ASP B 81 96.902 40.380 −25.749 1.00 20.00 6 ATOM 79 CB ASP B 81 96.888 41.192 −24.446 1.00 20.00 6 ATOM 80 CG ASP B 81 96.774 42.688 −24.682 1.00 20.00 6 ATOM 81 OD1 ASP B 81 97.436 43.193 −25.606 1.00 20.00 8 ATOM 82 OD2 ASP B 81 96.033 43.362 −23.933 1.00 20.00 8 ATOM 83 C ASP B 81 97.111 38.914 −25.393 1.00 20.00 6 ATOM 84 O ASP B 81 98.172 38.535 −24.890 1.00 20.00 8 ATOM 85 N PHE B 82 96.103 38.093 −25.679 1.00 20.00 7 ATOM 86 CA PHE B 82 96.140 36.677 −25.340 1.00 20.00 6 ATOM 87 CB PHE B 82 95.056 36.369 −24.302 1.00 20.00 6 ATOM 88 CG PHE B 82 95.157 37.187 −23.050 1.00 20.00 6 ATOM 89 CD1 PHE B 82 95.880 36.724 −21.959 1.00 20.00 6 ATOM 90 CD2 PHE B 82 94.525 38.423 −22.961 1.00 20.00 6 ATOM 91 CE1 PHE B 82 95.976 37.479 −20.793 1.00 20.00 6 ATOM 92 CE2 PHE B 82 94.615 39.188 −21.800 1.00 20.00 6 ATOM 93 CZ PHE B 82 95.343 38.712 −20.713 1.00 20.00 6 ATOM 94 C PHE B 82 95.929 35.719 −26.496 1.00 20.00 6 ATOM 95 O PHE B 82 95.342 36.061 −27.524 1.00 20.00 8 ATOM 96 N LYS B 83 96.406 34.500 −26.286 1.00 20.00 7 ATOM 97 CA LYS B 83 96.242 33.411 −27.228 1.00 20.00 6 ATOM 98 CB LYS B 83 97.594 32.777 −27.562 1.00 20.00 6 ATOM 99 CG LYS B 83 97.503 31.531 −28.425 1.00 20.00 6 ATOM 100 CD LYS B 83 98.888 31.074 −28.856 1.00 20.00 6 ATOM 101 CE LYS B 83 98.826 29.808 −29.699 1.00 20.00 6 ATOM 102 NZ LYS B 83 98.287 28.654 −28.918 1.00 20.00 7 ATOM 103 C LYS B 83 95.387 32.446 −26.416 1.00 20.00 6 ATOM 104 O LYS B 83 95.884 31.776 −25.510 1.00 20.00 8 ATOM 105 N PHE B 84 94.094 32.393 −26.710 1.00 20.00 7 ATOM 106 CA PHE B 84 93.217 31.511 −25.958 1.00 20.00 6 ATOM 107 CB PHE B 84 91.758 31.928 −26.133 1.00 20.00 6 ATOM 108 CG PHE B 84 91.426 33.228 −25.462 1.00 20.00 6 ATOM 109 CD1 PHE B 84 91.668 34.439 −26.099 1.00 20.00 6 ATOM 110 CD2 PHE B 84 90.907 33.243 −24.174 1.00 20.00 6 ATOM 111 CE1 PHE B 84 91.400 35.644 −25.464 1.00 20.00 6 ATOM 112 CE2 PHE B 84 90.636 34.447 −23.528 1.00 20.00 6 ATOM 113 CZ PHE B 84 90.884 35.646 −24.176 1.00 20.00 6 ATOM 114 C PHE B 84 93.402 30.054 −26.335 1.00 20.00 6 ATOM 115 O PHE B 84 93.734 29.734 −27.476 1.00 20.00 8 ATOM 116 N GLY B 85 93.196 29.178 −25.359 1.00 20.00 7 ATOM 117 CA GLY B 85 93.349 27.758 −25.591 1.00 20.00 6 ATOM 118 C GLY B 85 92.103 26.977 −25.221 1.00 20.00 6 ATOM 119 O GLY B 85 90.982 27.393 −25.525 1.00 20.00 8 ATOM 120 N LYS B 86 92.296 25.858 −24.534 1.00 20.00 7 ATOM 121 CA LYS B 86 91.182 25.005 −24.153 1.00 20.00 6 ATOM 122 CB LYS B 86 91.695 23.640 −23.687 1.00 20.00 6 ATOM 123 CG LYS B 86 92.421 23.667 −22.356 1.00 20.00 6 ATOM 124 CD LYS B 86 92.855 22.272 −21.941 1.00 20.00 6 ATOM 125 CE LYS B 86 93.685 22.319 −20.668 1.00 20.00 6 ATOM 126 NZ LYS B 86 94.209 20.975 −20.287 1.00 20.00 7 ATOM 127 C LYS B 86 90.267 25.576 −23.077 1.00 20.00 6 ATOM 128 O LYS B 86 90.668 26.410 −22.260 1.00 20.00 8 ATOM 129 N ILE B 87 89.026 25.106 −23.102 1.00 20.00 7 ATOM 130 CA ILE B 87 88.023 25.497 −22.131 1.00 20.00 6 ATOM 131 CB ILE B 87 86.604 25.159 −22.647 1.00 20.00 6 ATOM 132 CG2 ILE B 87 85.582 25.261 −21.503 1.00 20.00 6 ATOM 133 CG1 ILE B 87 86.260 26.085 −23.820 1.00 20.00 6 ATOM 134 CD1 ILE B 87 84.912 25.819 −24.463 1.00 20.00 6 ATOM 135 C ILE B 87 88.312 24.687 −20.872 1.00 20.00 6 ATOM 136 O ILE B 87 88.396 23.461 −20.927 1.00 20.00 8 ATOM 137 N LEU B 88 88.473 25.368 −19.742 1.00 20.00 7 ATOM 138 CA LEU B 88 88.757 24.686 −18.486 1.00 20.00 6 ATOM 139 CB LEU B 88 89.592 25.586 −17.575 1.00 20.00 6 ATOM 140 CG LEU B 88 90.968 25.987 −18.112 1.00 20.00 6 ATOM 141 CD1 LEU B 88 91.611 27.006 −17.186 1.00 20.00 6 ATOM 142 CD2 LEU B 88 91.836 24.756 −18.234 1.00 20.00 6 ATOM 143 C LEU B 88 87.471 24.298 −17.776 1.00 20.00 6 ATOM 144 O LEU B 88 87.434 23.334 −17.014 1.00 20.00 8 ATOM 145 N GLY B 89 86.410 25.051 −18.024 1.00 20.00 7 ATOM 146 CA GLY B 89 85.148 24.749 −17.382 1.00 20.00 6 ATOM 147 C GLY B 89 84.038 25.599 −17.953 1.00 20.00 6 ATOM 148 O GLY B 89 84.296 26.657 −18.541 1.00 20.00 8 ATOM 149 N GLU B 90 82.807 25.133 −17.781 1.00 20.00 7 ATOM 150 CA GLU B 90 81.629 25.832 −18.279 1.00 20.00 6 ATOM 151 CB GLU B 90 81.041 25.070 −19.471 1.00 20.00 6 ATOM 152 CG GLU B 90 81.929 25.084 −20.706 1.00 20.00 6 ATOM 153 CD GLU B 90 81.434 24.157 −21.802 1.00 20.00 6 ATOM 154 OE1 GLU B 90 81.539 22.923 −21.639 1.00 20.00 8 ATOM 155 OE2 GLU B 90 80.935 24.662 −22.827 1.00 20.00 8 ATOM 156 C GLU B 90 80.575 25.970 −17.188 1.00 20.00 6 ATOM 157 O GLU B 90 80.208 24.994 −16.543 1.00 20.00 8 ATOM 158 N GLY B 91 80.103 27.193 −16.979 1.00 20.00 7 ATOM 159 CA GLY B 91 79.080 27.431 −15.979 1.00 20.00 6 ATOM 160 C GLY B 91 77.835 27.949 −16.673 1.00 20.00 6 ATOM 161 O GLY B 91 77.804 28.046 −17.903 1.00 20.00 8 ATOM 162 N SER B 92 76.808 28.291 −15.904 1.00 20.00 7 ATOM 163 CA SER B 92 75.582 28.794 −16.508 1.00 20.00 6 ATOM 164 CB SER B 92 74.428 28.719 −15.505 1.00 20.00 6 ATOM 165 OG SER B 92 74.786 29.335 −14.282 1.00 20.00 8 ATOM 166 C SER B 92 75.726 30.219 −17.039 1.00 20.00 6 ATOM 167 O SER B 92 75.078 30.585 −18.018 1.00 20.00 8 ATOM 168 N PHE B 93 76.578 31.025 −16.411 1.00 20.00 7 ATOM 169 CA PHE B 93 76.763 32.399 −16.870 1.00 20.00 6 ATOM 170 CB PHE B 93 76.276 33.384 −15.807 1.00 20.00 6 ATOM 171 CG PHE B 93 74.832 33.220 −15.469 1.00 20.00 6 ATOM 172 CD1 PHE B 93 74.435 32.323 −14.483 1.00 20.00 6 ATOM 173 CD2 PHE B 93 73.859 33.914 −16.183 1.00 20.00 6 ATOM 174 CE1 PHE B 93 73.086 32.117 −14.210 1.00 20.00 6 ATOM 175 CE2 PHE B 93 72.507 33.715 −15.919 1.00 20.00 6 ATOM 176 CZ PHE B 93 72.120 32.812 −14.930 1.00 20.00 6 ATOM 177 C PHE B 93 78.197 32.736 −17.240 1.00 20.00 6 ATOM 178 O PHE B 93 78.543 33.908 −17.397 1.00 20.00 8 ATOM 179 N SER B 94 79.030 31.713 −17.394 1.00 20.00 7 ATOM 180 CA SER B 94 80.421 31.948 −17.735 1.00 20.00 6 ATOM 181 CB SER B 94 81.174 32.443 −16.503 1.00 20.00 6 ATOM 182 OG SER B 94 81.237 31.410 −15.535 1.00 20.00 8 ATOM 183 C SER B 94 81.123 30.707 −18.253 1.00 20.00 6 ATOM 184 O SER B 94 80.666 29.584 −18.048 1.00 20.00 8 ATOM 185 N THR B 95 82.252 30.937 −18.913 1.00 20.00 7 ATOM 186 CA THR B 95 83.088 29.879 −19.455 1.00 20.00 6 ATOM 187 CB THR B 95 82.942 29.770 −20.985 1.00 20.00 6 ATOM 188 OG1 THR B 95 81.589 29.425 −21.309 1.00 20.00 8 ATOM 189 CG2 THR B 95 83.873 28.694 −21.536 1.00 20.00 6 ATOM 190 C THR B 95 84.524 30.264 −19.118 1.00 20.00 6 ATOM 191 O THR B 95 84.957 31.388 −19.399 1.00 20.00 8 ATOM 192 N VAL B 96 85.257 29.348 −18.498 1.00 20.00 7 ATOM 193 CA VAL B 96 86.642 29.628 −18.141 1.00 20.00 6 ATOM 194 CB VAL B 96 86.991 29.050 −16.761 1.00 20.00 6 ATOM 195 CG1 VAL B 96 88.438 29.390 −16.407 1.00 20.00 6 ATOM 196 CG2 VAL B 96 86.041 29.627 −15.707 1.00 20.00 6 ATOM 197 C VAL B 96 87.541 29.027 −19.210 1.00 20.00 6 ATOM 198 O VAL B 96 87.432 27.845 −19.540 1.00 20.00 8 ATOM 199 N VAL B 97 88.416 29.858 −19.763 1.00 20.00 7 ATOM 200 CA VAL B 97 89.312 29.430 −20.824 1.00 20.00 6 ATOM 201 CB VAL B 97 89.006 30.194 −22.130 1.00 20.00 6 ATOM 202 CG1 VAL B 97 89.828 29.624 −23.279 1.00 20.00 6 ATOM 203 CG2 VAL B 97 87.515 30.116 −22.444 1.00 20.00 6 ATOM 204 C VAL B 97 90.771 29.664 −20.458 1.00 20.00 6 ATOM 205 O VAL B 97 91.122 30.698 −19.889 1.00 20.00 8 ATOM 206 N LEU B 98 91.617 28.690 −20.770 1.00 20.00 7 ATOM 207 CA LEU B 98 93.039 28.821 −20.499 1.00 20.00 6 ATOM 208 CB LEU B 98 93.727 27.459 −20.618 1.00 20.00 6 ATOM 209 CG LEU B 98 95.240 27.421 −20.383 1.00 20.00 6 ATOM 210 CD1 LEU B 98 95.565 28.019 −19.021 1.00 20.00 6 ATOM 211 CD2 LEU B 98 95.739 25.987 −20.463 1.00 20.00 6 ATOM 212 C LEU B 98 93.580 29.785 −21.552 1.00 20.00 6 ATOM 213 O LEU B 98 93.293 29.637 −22.738 1.00 20.00 8 ATOM 214 N ALA B 99 94.343 30.783 −21.121 1.00 20.00 7 ATOM 215 CA ALA B 99 94.897 31.767 −22.043 1.00 20.00 6 ATOM 216 CB ALA B 99 94.087 33.055 −21.980 1.00 20.00 6 ATOM 217 C ALA B 99 96.353 32.067 −21.723 1.00 20.00 6 ATOM 218 O ALA B 99 96.748 32.110 −20.554 1.00 20.00 8 ATOM 219 N ARG B 100 97.152 32.270 −22.763 1.00 20.00 7 ATOM 220 CA ARG B 100 98.554 32.596 −22.568 1.00 20.00 6 ATOM 221 CB ARG B 100 99.442 31.657 −23.393 1.00 20.00 6 ATOM 222 CG ARG B 100 100.934 31.833 −23.131 1.00 20.00 6 ATOM 223 CD ARG B 100 101.770 30.835 −23.923 1.00 20.00 6 ATOM 224 NE ARG B 100 101.600 29.452 −23.469 1.00 20.00 7 ATOM 225 CZ ARG B 100 102.059 28.970 −22.314 1.00 20.00 6 ATOM 226 NH1 ARG B 100 102.722 29.752 −21.473 1.00 20.00 7 ATOM 227 NH2 ARG B 100 101.864 27.694 −22.003 1.00 20.00 7 ATOM 228 C ARG B 100 98.756 34.045 −23.004 1.00 20.00 6 ATOM 229 O ARG B 100 98.454 34.408 −24.146 1.00 20.00 8 ATOM 230 N GLU B 101 99.228 34.883 −22.087 1.00 20.00 7 ATOM 231 CA GLU B 101 99.470 36.286 −22.408 1.00 20.00 6 ATOM 232 CB GLU B 101 99.709 37.091 −21.123 1.00 20.00 6 ATOM 233 CG GLU B 101 99.986 38.571 −21.363 1.00 20.00 6 ATOM 234 CD GLU B 101 100.164 39.347 −20.075 1.00 20.00 6 ATOM 235 OE1 GLU B 101 100.717 38.780 −19.114 1.00 20.00 8 ATOM 236 OE2 GLU B 101 99.765 40.531 −20.025 1.00 20.00 8 ATOM 237 C GLU B 101 100.703 36.338 −23.317 1.00 20.00 6 ATOM 238 O GLU B 101 101.773 35.865 −22.944 1.00 20.00 8 ATOM 239 N LEU B 102 100.546 36.909 −24.507 1.00 20.00 7 ATOM 240 CA LEU B 102 101.632 36.982 −25.482 1.00 20.00 6 ATOM 241 CB LEU B 102 101.145 37.683 −26.753 1.00 20.00 6 ATOM 242 CG LEU B 102 100.013 36.985 −27.517 1.00 20.00 6 ATOM 243 CD1 LEU B 102 99.500 37.897 −28.623 1.00 20.00 6 ATOM 244 CD2 LEU B 102 100.517 35.670 −28.089 1.00 20.00 6 ATOM 245 C LEU B 102 102.906 37.663 −25.000 1.00 20.00 6 ATOM 246 O LEU B 102 104.000 37.137 −25.180 1.00 20.00 8 ATOM 247 N ALA B 103 102.760 38.828 −24.382 1.00 20.00 7 ATOM 248 CA ALA B 103 103.909 39.587 −23.910 1.00 20.00 6 ATOM 249 CB ALA B 103 103.464 41.002 −23.546 1.00 20.00 6 ATOM 250 C ALA B 103 104.697 38.983 −22.747 1.00 20.00 6 ATOM 251 O ALA B 103 105.832 39.389 −22.503 1.00 20.00 8 ATOM 252 N THR B 104 104.122 38.007 −22.050 1.00 20.00 7 ATOM 253 CA THR B 104 104.790 37.418 −20.893 1.00 20.00 6 ATOM 254 CB THR B 104 104.059 37.799 −19.592 1.00 20.00 6 ATOM 255 OG1 THR B 104 102.712 37.303 −19.648 1.00 20.00 8 ATOM 256 CG2 THR B 104 104.033 39.313 −19.404 1.00 20.00 6 ATOM 257 C THR B 104 104.880 35.902 −20.901 1.00 20.00 6 ATOM 258 O THR B 104 105.677 35.323 −20.160 1.00 20.00 8 ATOM 259 N SER B 105 104.042 35.274 −21.722 1.00 20.00 7 ATOM 260 CA SER B 105 103.950 33.818 −21.842 1.00 20.00 6 ATOM 261 CB SER B 105 105.344 33.213 −22.048 1.00 20.00 6 ATOM 262 OG SER B 105 105.264 31.819 −22.287 1.00 20.00 8 ATOM 263 C SER B 105 103.304 33.243 −20.576 1.00 20.00 6 ATOM 264 O SER B 105 103.286 32.029 −20.363 1.00 20.00 8 ATOM 265 N ARG B 106 102.771 34.124 −19.736 1.00 20.00 7 ATOM 266 CA ARG B 106 102.089 33.709 −18.509 1.00 20.00 6 ATOM 267 CB ARG B 106 101.833 34.914 −17.598 1.00 20.00 6 ATOM 268 CG ARG B 106 103.022 35.361 −16.781 1.00 20.00 6 ATOM 269 CD ARG B 106 102.724 36.653 −16.045 1.00 20.00 6 ATOM 270 NE ARG B 106 103.756 36.940 −15.051 1.00 20.00 7 ATOM 271 CZ ARG B 106 103.964 38.132 −14.504 1.00 20.00 6 ATOM 272 NH1 ARG B 106 103.210 39.167 −14.858 1.00 20.00 7 ATOM 273 NH2 ARG B 106 104.918 38.279 −13.590 1.00 20.00 7 ATOM 274 C ARG B 106 100.743 33.082 −18.856 1.00 20.00 6 ATOM 275 O ARG B 106 100.069 33.534 −19.777 1.00 20.00 8 ATOM 276 N GLU B 107 100.354 32.049 −18.115 1.00 20.00 7 ATOM 277 CA GLU B 107 99.072 31.390 −18.336 1.00 20.00 6 ATOM 278 CB GLU B 107 99.193 29.870 −18.212 1.00 20.00 6 ATOM 279 CG GLU B 107 100.180 29.207 −19.144 1.00 20.00 6 ATOM 280 CD GLU B 107 100.124 27.696 −19.023 1.00 20.00 6 ATOM 281 OE1 GLU B 107 99.373 27.068 −19.798 1.00 20.00 8 ATOM 282 OE2 GLU B 107 100.813 27.144 −18.138 1.00 20.00 8 ATOM 283 C GLU B 107 98.070 31.848 −17.285 1.00 20.00 6 ATOM 284 O GLU B 107 98.368 31.833 −16.095 1.00 20.00 8 ATOM 285 N TYR B 108 96.885 32.243 −17.727 1.00 20.00 7 ATOM 286 CA TYR B 108 95.829 32.667 −16.817 1.00 20.00 6 ATOM 287 CB TYR B 108 95.525 34.156 −16.979 1.00 20.00 6 ATOM 288 CG TYR B 108 96.603 35.089 −16.487 1.00 20.00 6 ATOM 289 CD1 TYR B 108 96.744 35.369 −15.129 1.00 20.00 6 ATOM 290 CE1 TYR B 108 97.727 36.260 −14.674 1.00 20.00 6 ATOM 291 CD2 TYR B 108 97.467 35.712 −17.386 1.00 20.00 6 ATOM 292 CE2 TYR B 108 98.442 36.597 −16.950 1.00 20.00 6 ATOM 293 CZ TYR B 108 98.569 36.869 −15.599 1.00 20.00 6 ATOM 294 OH TYR B 108 99.529 37.756 −15.187 1.00 20.00 8 ATOM 295 C TYR B 108 94.566 31.899 −17.167 1.00 20.00 6 ATOM 296 O TYR B 108 94.389 31.463 −18.306 1.00 20.00 8 ATOM 297 N ALA B 109 93.697 31.723 −16.181 1.00 20.00 7 ATOM 298 CA ALA B 109 92.421 31.073 −16.414 1.00 20.00 6 ATOM 299 CB ALA B 109 92.024 30.225 −15.214 1.00 20.00 6 ATOM 300 C ALA B 109 91.513 32.288 −16.542 1.00 20.00 6 ATOM 301 O ALA B 109 91.278 33.003 −15.558 1.00 20.00 8 ATOM 302 N ILE B 110 91.042 32.557 −17.756 1.00 20.00 7 ATOM 303 CA ILE B 110 90.186 33.711 −17.968 1.00 20.00 6 ATOM 304 CB ILE B 110 90.574 34.462 −19.271 1.00 20.00 6 ATOM 305 CG2 ILE B 110 89.628 35.630 −19.507 1.00 20.00 6 ATOM 306 CG1 ILE B 110 92.023 34.962 −19.159 1.00 20.00 6 ATOM 307 CD1 ILE B 110 92.487 35.847 −20.312 1.00 20.00 6 ATOM 308 C ILE B 110 88.715 33.318 −18.004 1.00 20.00 6 ATOM 309 O ILE B 110 88.285 32.527 −18.851 1.00 20.00 8 ATOM 310 N LYS B 111 87.956 33.852 −17.052 1.00 20.00 7 ATOM 311 CA LYS B 111 86.527 33.581 −16.975 1.00 20.00 6 ATOM 312 CB LYS B 111 86.022 33.721 −15.531 1.00 20.00 6 ATOM 313 CG LYS B 111 84.509 33.598 −15.411 1.00 20.00 6 ATOM 314 CD LYS B 111 84.025 33.590 −13.965 1.00 20.00 6 ATOM 315 CE LYS B 111 84.318 32.262 −13.277 1.00 20.00 6 ATOM 316 NZ LYS B 111 83.784 32.217 −11.875 1.00 20.00 7 ATOM 317 C LYS B 111 85.844 34.601 −17.869 1.00 20.00 6 ATOM 318 O LYS B 111 86.017 35.807 −17.688 1.00 20.00 8 ATOM 319 N ILE B 112 85.078 34.111 −18.838 1.00 20.00 7 ATOM 320 CA ILE B 112 84.383 34.976 −19.782 1.00 20.00 6 ATOM 321 CB ILE B 112 84.695 34.548 −21.233 1.00 20.00 6 ATOM 322 CG2 ILE B 112 84.042 35.505 −22.216 1.00 20.00 6 ATOM 323 CG1 ILE B 112 86.216 34.518 −21.440 1.00 20.00 6 ATOM 324 CD1 ILE B 112 86.657 33.949 −22.779 1.00 20.00 6 ATOM 325 C ILE B 112 82.878 34.916 −19.538 1.00 20.00 6 ATOM 326 O ILE B 112 82.288 33.839 −19.510 1.00 20.00 8 ATOM 327 N LEU B 113 82.269 36.083 −19.347 1.00 20.00 7 ATOM 328 CA LEU B 113 80.835 36.172 −19.089 1.00 20.00 6 ATOM 329 CB LEU B 113 80.585 36.696 −17.669 1.00 20.00 6 ATOM 330 CG LEU B 113 81.350 36.038 −16.521 1.00 20.00 6 ATOM 331 CD1 LEU B 113 82.743 36.638 −16.428 1.00 20.00 6 ATOM 332 CD2 LEU B 113 80.609 36.258 −15.215 1.00 20.00 6 ATOM 333 C LEU B 113 80.172 37.110 −20.090 1.00 20.00 6 ATOM 334 O LEU B 113 80.634 38.232 −20.299 1.00 20.00 8 ATOM 335 N GLU B 114 79.088 36.653 −20.709 1.00 20.00 7 ATOM 336 CA GLU B 114 78.377 37.472 −21.681 1.00 20.00 6 ATOM 337 CB GLU B 114 77.514 36.586 −22.581 1.00 20.00 6 ATOM 338 CG GLU B 114 76.670 37.366 −23.571 1.00 20.00 6 ATOM 339 CD GLU B 114 75.749 36.473 −24.372 1.00 20.00 6 ATOM 340 OE1 GLU B 114 75.083 35.613 −23.760 1.00 20.00 8 ATOM 341 OE2 GLU B 114 75.684 36.638 −25.611 1.00 20.00 8 ATOM 342 C GLU B 114 77.509 38.491 −20.942 1.00 20.00 6 ATOM 343 O GLU B 114 76.673 38.122 −20.113 1.00 20.00 8 ATOM 344 N LYS B 115 77.709 39.771 −21.235 1.00 20.00 7 ATOM 345 CA LYS B 115 76.945 40.808 −20.553 1.00 20.00 6 ATOM 346 CB LYS B 115 77.433 42.202 −20.978 1.00 20.00 6 ATOM 347 CG LYS B 115 78.653 42.675 −20.183 1.00 20.00 6 ATOM 348 CD LYS B 115 79.174 44.045 −20.618 1.00 20.00 6 ATOM 349 CE LYS B 115 79.832 43.994 −21.992 1.00 20.00 6 ATOM 350 NZ LYS B 115 80.536 45.273 −22.323 1.00 20.00 7 ATOM 351 C LYS B 115 75.435 40.693 −20.743 1.00 20.00 6 ATOM 352 O LYS B 115 74.676 40.787 −19.778 1.00 20.00 8 ATOM 353 N ARG B 116 74.997 40.471 −21.977 1.00 20.00 7 ATOM 354 CA ARG B 116 73.570 40.363 −22.255 1.00 20.00 6 ATOM 355 CB ARG B 116 73.346 40.066 −23.743 1.00 20.00 6 ATOM 356 CG ARG B 116 71.893 39.821 −24.142 1.00 20.00 6 ATOM 357 CD ARG B 116 70.931 40.791 −23.465 1.00 20.00 6 ATOM 358 NE ARG B 116 71.401 42.172 −23.493 1.00 20.00 7 ATOM 359 CZ ARG B 116 70.780 43.177 −22.884 1.00 20.00 6 ATOM 360 NH1 ARG B 116 69.663 42.949 −22.207 1.00 20.00 7 ATOM 361 NH2 ARG B 116 71.278 44.405 −22.942 1.00 20.00 7 ATOM 362 C ARG B 116 72.888 39.298 −21.394 1.00 20.00 6 ATOM 363 O ARG B 116 71.862 39.567 −20.764 1.00 20.00 8 ATOM 364 N HIS B 117 73.463 38.101 −21.347 1.00 20.00 7 ATOM 365 CA HIS B 117 72.885 37.020 −20.556 1.00 20.00 6 ATOM 366 CB HIS B 117 73.704 35.738 −20.723 1.00 20.00 6 ATOM 367 CG HIS B 117 73.053 34.525 −20.133 1.00 20.00 6 ATOM 368 CD2 HIS B 117 71.762 34.274 −19.810 1.00 20.00 6 ATOM 369 ND1 HIS B 117 73.752 33.376 −19.836 1.00 20.00 7 ATOM 370 CE1 HIS B 117 72.921 32.467 −19.355 1.00 20.00 6 ATOM 371 NE2 HIS B 117 71.707 32.987 −19.330 1.00 20.00 7 ATOM 372 C HIS B 117 72.816 37.386 −19.077 1.00 20.00 6 ATOM 373 O HIS B 117 71.823 37.113 −18.409 1.00 20.00 8 ATOM 374 N ILE B 118 73.882 37.992 −18.564 1.00 20.00 7 ATOM 375 CA ILE B 118 73.927 38.391 −17.160 1.00 20.00 6 ATOM 376 CB ILE B 118 75.269 39.073 −16.827 1.00 20.00 6 ATOM 377 CG2 ILE B 118 75.180 39.787 −15.486 1.00 20.00 6 ATOM 378 CG1 ILE B 118 76.392 38.029 −16.834 1.00 20.00 6 ATOM 379 CD1 ILE B 118 77.784 38.625 −16.709 1.00 20.00 6 ATOM 380 C ILE B 118 72.788 39.353 −16.833 1.00 20.00 6 ATOM 381 O ILE B 118 72.101 39.196 −15.827 1.00 20.00 8 ATOM 382 N ILE B 119 72.596 40.349 −17.690 1.00 20.00 7 ATOM 383 CA ILE B 119 71.538 41.333 −17.494 1.00 20.00 6 ATOM 384 CB ILE B 119 71.646 42.473 −18.539 1.00 20.00 6 ATOM 385 CG2 ILE B 119 70.396 43.357 −18.492 1.00 20.00 6 ATOM 386 CG1 ILE B 119 72.919 43.292 −18.270 1.00 20.00 6 ATOM 387 CD1 ILE B 119 73.212 44.370 −19.314 1.00 20.00 6 ATOM 388 C ILE B 119 70.154 40.687 −17.580 1.00 20.00 6 ATOM 389 O ILE B 119 69.289 40.953 −16.747 1.00 20.00 8 ATOM 390 N LYS B 120 69.950 39.832 −18.579 1.00 20.00 7 ATOM 391 CA LYS B 120 68.659 39.169 −18.754 1.00 20.00 6 ATOM 392 CB LYS B 120 68.697 38.200 −19.935 1.00 20.00 6 ATOM 393 CG LYS B 120 68.942 38.841 −21.284 1.00 20.00 6 ATOM 394 CD LYS B 120 68.926 37.782 −22.387 1.00 20.00 6 ATOM 395 CE LYS B 120 69.934 36.665 −22.093 1.00 20.00 6 ATOM 396 NZ LYS B 120 69.950 35.599 −23.127 1.00 20.00 7 ATOM 397 C LYS B 120 68.229 38.398 −17.513 1.00 20.00 6 ATOM 398 O LYS B 120 67.077 38.490 −17.092 1.00 20.00 8 ATOM 399 N GLU B 121 69.154 37.639 −16.930 1.00 20.00 7 ATOM 400 CA GLU B 121 68.851 36.839 −15.747 1.00 20.00 6 ATOM 401 CB GLU B 121 69.678 35.549 −15.758 1.00 20.00 6 ATOM 402 CG GLU B 121 69.485 34.674 −16.995 1.00 20.00 6 ATOM 403 CD GLU B 121 68.029 34.326 −17.248 1.00 20.00 6 ATOM 404 OE1 GLU B 121 67.339 33.904 −16.295 1.00 20.00 8 ATOM 405 OE2 GLU B 121 67.574 34.470 −18.404 1.00 20.00 8 ATOM 406 C GLU B 121 69.071 37.573 −14.424 1.00 20.00 6 ATOM 407 O GLU B 121 69.117 36.946 −13.362 1.00 20.00 8 ATOM 408 N ASN B 122 69.208 38.895 −14.485 1.00 20.00 7 ATOM 409 CA ASN B 122 69.411 39.699 −13.281 1.00 20.00 6 ATOM 410 CB ASN B 122 68.132 39.715 −12.439 1.00 20.00 6 ATOM 411 CG ASN B 122 66.952 40.314 −13.177 1.00 20.00 6 ATOM 412 OD1 ASN B 122 66.428 39.725 −14.121 1.00 20.00 8 ATOM 413 ND2 ASN B 122 66.530 41.498 −12.748 1.00 20.00 7 ATOM 414 C ASN B 122 70.563 39.180 −12.419 1.00 20.00 6 ATOM 415 O ASN B 122 70.408 39.007 −11.212 1.00 20.00 8 ATOM 416 N LYS B 123 71.716 38.942 −13.033 1.00 20.00 7 ATOM 417 CA LYS B 123 72.870 38.434 −12.301 1.00 20.00 6 ATOM 418 CB LYS B 123 73.500 37.266 −13.065 1.00 20.00 6 ATOM 419 CG LYS B 123 72.568 36.086 −13.276 1.00 20.00 6 ATOM 420 CD LYS B 123 72.065 35.539 −11.948 1.00 20.00 6 ATOM 421 CE LYS B 123 71.032 34.445 −12.159 1.00 20.00 6 ATOM 422 NZ LYS B 123 70.421 34.016 −10.871 1.00 20.00 7 ATOM 423 C LYS B 123 73.931 39.498 −12.054 1.00 20.00 6 ATOM 424 O LYS B 123 75.035 39.183 −11.611 1.00 20.00 8 ATOM 425 N VAL B 124 73.607 40.753 −12.340 1.00 20.00 7 ATOM 426 CA VAL B 124 74.575 41.822 −12.145 1.00 20.00 6 ATOM 427 CB VAL B 124 73.997 43.201 −12.547 1.00 20.00 6 ATOM 428 CG1 VAL B 124 75.035 44.290 −12.302 1.00 20.00 6 ATOM 429 CG2 VAL B 124 73.608 43.186 −14.022 1.00 20.00 6 ATOM 430 C VAL B 124 75.091 41.885 −10.712 1.00 20.00 6 ATOM 431 O VAL B 124 76.278 42.115 −10.490 1.00 20.00 8 ATOM 432 N PRO B 125 74.207 41.695 −9.716 1.00 20.00 7 ATOM 433 CD PRO B 125 72.735 41.613 −9.757 1.00 20.00 6 ATOM 434 CA PRO B 125 74.688 41.747 −8.331 1.00 20.00 6 ATOM 435 CB PRO B 125 73.411 41.558 −7.512 1.00 20.00 6 ATOM 436 CG PRO B 125 72.346 42.152 −8.396 1.00 20.00 6 ATOM 437 C PRO B 125 75.715 40.643 −8.051 1.00 20.00 6 ATOM 438 O PRO B 125 76.683 40.851 −7.325 1.00 20.00 8 ATOM 439 N TYR B 126 75.493 39.475 −8.640 1.00 20.00 7 ATOM 440 CA TYR B 126 76.380 38.334 −8.440 1.00 20.00 6 ATOM 441 CB TYR B 126 75.699 37.059 −8.942 1.00 20.00 6 ATOM 442 CG TYR B 126 74.479 36.687 −8.127 1.00 20.00 6 ATOM 443 CD1 TYR B 126 74.611 36.068 −6.884 1.00 20.00 6 ATOM 444 CE1 TYR B 126 73.491 35.748 −6.112 1.00 20.00 6 ATOM 445 CD2 TYR B 126 73.193 36.981 −8.583 1.00 20.00 6 ATOM 446 CE2 TYR B 126 72.063 36.667 −7.817 1.00 20.00 6 ATOM 447 CZ TYR B 126 72.223 36.052 −6.584 1.00 20.00 6 ATOM 448 OH TYR B 126 71.118 35.743 −5.823 1.00 20.00 8 ATOM 449 C TYR B 126 77.738 38.511 −9.113 1.00 20.00 6 ATOM 450 O TYR B 126 78.777 38.273 −8.492 1.00 20.00 8 ATOM 451 N VAL B 127 77.738 38.931 −10.374 1.00 20.00 7 ATOM 452 CA VAL B 127 78.994 39.123 −11.085 1.00 20.00 6 ATOM 453 CB VAL B 127 78.756 39.466 −12.567 1.00 20.00 6 ATOM 454 CG1 VAL B 127 80.096 39.637 −13.275 1.00 20.00 6 ATOM 455 CG2 VAL B 127 77.949 38.357 −13.234 1.00 20.00 6 ATOM 456 C VAL B 127 79.798 40.242 −10.427 1.00 20.00 6 ATOM 457 O VAL B 127 81.016 40.148 −10.292 1.00 20.00 8 ATOM 458 N THR B 128 79.105 41.293 −10.006 1.00 20.00 7 ATOM 459 CA THR B 128 79.746 42.424 −9.345 1.00 20.00 6 ATOM 460 CB THR B 128 78.721 43.548 −9.070 1.00 20.00 6 ATOM 461 OG1 THR B 128 78.194 44.025 −10.316 1.00 20.00 8 ATOM 462 CG2 THR B 128 79.371 44.703 −8.330 1.00 20.00 6 ATOM 463 C THR B 128 80.372 41.979 −8.019 1.00 20.00 6 ATOM 464 O THR B 128 81.500 42.355 −7.696 1.00 20.00 8 ATOM 465 N ARG B 129 79.637 41.172 −7.256 1.00 20.00 7 ATOM 466 CA ARG B 129 80.126 40.678 −5.971 1.00 20.00 6 ATOM 467 CB ARG B 129 79.035 39.888 −5.254 1.00 20.00 6 ATOM 468 CG ARG B 129 79.428 39.438 −3.852 1.00 20.00 6 ATOM 469 CD ARG B 129 78.351 38.554 −3.278 1.00 20.00 6 ATOM 470 NE ARG B 129 77.048 39.209 −3.315 1.00 20.00 7 ATOM 471 CZ ARG B 129 75.894 38.569 −3.484 1.00 20.00 6 ATOM 472 NH1 ARG B 129 75.878 37.250 −3.636 1.00 20.00 7 ATOM 473 NH2 ARG B 129 74.756 39.248 −3.501 1.00 20.00 7 ATOM 474 C ARG B 129 81.354 39.788 −6.146 1.00 20.00 6 ATOM 475 O ARG B 129 82.315 39.885 −5.379 1.00 20.00 8 ATOM 476 N GLU B 130 81.316 38.917 −7.151 1.00 20.00 7 ATOM 477 CA GLU B 130 82.439 38.029 −7.421 1.00 20.00 6 ATOM 478 CB GLU B 130 82.191 37.211 −8.692 1.00 20.00 6 ATOM 479 CG GLU B 130 83.408 36.427 −9.167 1.00 20.00 6 ATOM 480 CD GLU B 130 83.060 35.338 −10.168 1.00 20.00 6 ATOM 481 OE1 GLU B 130 82.227 35.590 −11.061 1.00 20.00 8 ATOM 482 OE2 GLU B 130 83.626 34.231 −10.068 1.00 20.00 8 ATOM 483 C GLU B 130 83.708 38.853 −7.580 1.00 20.00 6 ATOM 484 O GLU B 130 84.723 38.575 −6.940 1.00 20.00 8 ATOM 485 N ARG B 131 83.641 39.874 −8.428 1.00 20.00 7 ATOM 486 CA ARG B 131 84.788 40.742 −8.673 1.00 20.00 6 ATOM 487 CB ARG B 131 84.459 41.759 −9.777 1.00 20.00 6 ATOM 488 CG ARG B 131 85.580 42.753 −10.035 1.00 20.00 6 ATOM 489 CD ARG B 131 85.262 43.716 −11.167 1.00 20.00 6 ATOM 490 NE ARG B 131 86.351 44.673 −11.355 1.00 20.00 7 ATOM 491 CZ ARG B 131 86.416 45.561 −12.343 1.00 20.00 6 ATOM 492 NH1 ARG B 131 85.450 45.623 −13.250 1.00 20.00 7 ATOM 493 NH2 ARG B 131 87.450 46.388 −12.426 1.00 20.00 7 ATOM 494 C ARG B 131 85.228 41.485 −7.409 1.00 20.00 6 ATOM 495 O ARG B 131 86.413 41.500 −7.071 1.00 20.00 8 ATOM 496 N ASP B 132 84.277 42.103 −6.715 1.00 20.00 7 ATOM 497 CA ASP B 132 84.594 42.848 −5.505 1.00 20.00 6 ATOM 498 CB ASP B 132 83.350 43.575 −4.987 1.00 20.00 6 ATOM 499 CG ASP B 132 82.865 44.658 −5.943 1.00 20.00 6 ATOM 500 OD1 ASP B 132 83.612 45.010 −6.886 1.00 20.00 8 ATOM 501 OD2 ASP B 132 81.739 45.167 −5.747 1.00 20.00 8 ATOM 502 C ASP B 132 85.192 41.969 −4.401 1.00 20.00 6 ATOM 503 O ASP B 132 86.191 42.337 −3.783 1.00 20.00 8 ATOM 504 N VAL B 133 84.596 40.809 −4.150 1.00 20.00 7 ATOM 505 CA VAL B 133 85.131 39.933 −3.116 1.00 20.00 6 ATOM 506 CB VAL B 133 84.226 38.698 −2.885 1.00 20.00 6 ATOM 507 CG1 VAL B 133 84.920 37.713 −1.957 1.00 20.00 6 ATOM 508 CG2 VAL B 133 82.893 39.135 −2.271 1.00 20.00 6 ATOM 509 C VAL B 133 86.540 39.470 −3.477 1.00 20.00 6 ATOM 510 O VAL B 133 87.460 39.602 −2.675 1.00 20.00 8 ATOM 511 N MET B 134 86.721 38.950 −4.688 1.00 20.00 7 ATOM 512 CA MET B 134 88.040 38.474 −5.083 1.00 20.00 6 ATOM 513 CB MET B 134 88.004 37.879 −6.492 1.00 20.00 6 ATOM 514 CG MET B 134 87.183 36.603 −6.573 1.00 20.00 6 ATOM 515 SD MET B 134 87.477 35.650 −8.077 1.00 20.00 16  ATOM 516 CE MET B 134 88.730 34.515 −7.475 1.00 20.00 6 ATOM 517 C MET B 134 89.115 39.552 −4.994 1.00 20.00 6 ATOM 518 O MET B 134 90.253 39.264 −4.626 1.00 20.00 8 ATOM 519 N SER B 135 88.758 40.790 −5.319 1.00 20.00 7 ATOM 520 CA SER B 135 89.708 41.899 −5.260 1.00 20.00 6 ATOM 521 CB SER B 135 89.084 43.175 −5.836 1.00 20.00 6 ATOM 522 OG SER B 135 88.742 43.009 −7.202 1.00 20.00 8 ATOM 523 C SER B 135 90.165 42.184 −3.830 1.00 20.00 6 ATOM 524 O SER B 135 91.228 42.762 −3.614 1.00 20.00 8 ATOM 525 N ARG B 136 89.354 41.782 −2.857 1.00 20.00 7 ATOM 526 CA ARG B 136 89.672 42.013 −1.450 1.00 20.00 6 ATOM 527 CB ARG B 136 88.384 42.156 −0.637 1.00 20.00 6 ATOM 528 CG ARG B 136 87.509 43.336 −1.018 1.00 20.00 6 ATOM 529 CD ARG B 136 86.215 43.306 −0.211 1.00 20.00 6 ATOM 530 NE ARG B 136 86.491 43.117 1.209 1.00 20.00 7 ATOM 531 CZ ARG B 136 85.565 42.888 2.132 1.00 20.00 6 ATOM 532 NH1 ARG B 136 84.285 42.821 1.786 1.00 20.00 7 ATOM 533 NH2 ARG B 136 85.920 42.715 3.401 1.00 20.00 7 ATOM 534 C ARG B 136 90.506 40.891 −0.839 1.00 20.00 6 ATOM 535 O ARG B 136 91.091 41.054 0.231 1.00 20.00 8 ATOM 536 N LEU B 137 90.556 39.752 −1.515 1.00 20.00 7 ATOM 537 CA LEU B 137 91.300 38.609 −1.005 1.00 20.00 6 ATOM 538 CB LEU B 137 90.665 37.307 −1.504 1.00 20.00 6 ATOM 539 CG LEU B 137 89.172 37.099 −1.213 1.00 20.00 6 ATOM 540 CD1 LEU B 137 88.748 35.728 −1.734 1.00 20.00 6 ATOM 541 CD2 LEU B 137 88.897 37.205 0.280 1.00 20.00 6 ATOM 542 C LEU B 137 92.771 38.648 −1.402 1.00 20.00 6 ATOM 543 O LEU B 137 93.103 38.871 −2.566 1.00 20.00 8 ATOM 544 N ASP B 138 93.645 38.436 −0.424 1.00 20.00 7 ATOM 545 CA ASP B 138 95.086 38.422 −0.656 1.00 20.00 6 ATOM 546 CB ASP B 138 95.696 39.797 −0.352 1.00 20.00 6 ATOM 547 CG ASP B 138 97.179 39.854 −0.674 1.00 20.00 6 ATOM 548 OD1 ASP B 138 97.601 39.173 −1.634 1.00 20.00 8 ATOM 549 OD2 ASP B 138 97.920 40.581 0.022 1.00 20.00 8 ATOM 550 C ASP B 138 95.678 37.369 0.263 1.00 20.00 6 ATOM 551 O ASP B 138 96.353 37.685 1.243 1.00 20.00 8 ATOM 552 N HIS B 139 95.410 36.111 −0.065 1.00 20.00 7 ATOM 553 CA HIS B 139 95.871 34.984 0.731 1.00 20.00 6 ATOM 554 CB HIS B 139 94.769 34.610 1.737 1.00 20.00 6 ATOM 555 CG HIS B 139 95.173 33.561 2.725 1.00 20.00 6 ATOM 556 CD2 HIS B 139 95.543 33.657 4.025 1.00 20.00 6 ATOM 557 ND1 HIS B 139 95.241 32.221 2.405 1.00 20.00 7 ATOM 558 CE1 HIS B 139 95.635 31.537 3.466 1.00 20.00 6 ATOM 559 NE2 HIS B 139 95.825 32.385 4.461 1.00 20.00 7 ATOM 560 C HIS B 139 96.176 33.828 −0.221 1.00 20.00 6 ATOM 561 O HIS B 139 95.444 33.595 −1.182 1.00 20.00 8 ATOM 562 N PRO B 140 97.257 33.080 0.038 1.00 20.00 7 ATOM 563 CD PRO B 140 98.128 33.140 1.225 1.00 20.00 6 ATOM 564 CA PRO B 140 97.635 31.959 −0.827 1.00 20.00 6 ATOM 565 CB PRO B 140 98.913 31.433 −0.171 1.00 20.00 6 ATOM 566 CG PRO B 140 98.687 31.730 1.277 1.00 20.00 6 ATOM 567 C PRO B 140 96.614 30.846 −1.072 1.00 20.00 6 ATOM 568 O PRO B 140 96.747 30.107 −2.044 1.00 20.00 8 ATOM 569 N PHE B 141 95.607 30.712 −0.211 1.00 20.00 7 ATOM 570 CA PHE B 141 94.620 29.649 −0.398 1.00 20.00 6 ATOM 571 CB PHE B 141 94.206 29.056 0.961 1.00 20.00 6 ATOM 572 CG PHE B 141 95.321 28.335 1.681 1.00 20.00 6 ATOM 573 CD1 PHE B 141 96.351 27.716 0.967 1.00 20.00 6 ATOM 574 CD2 PHE B 141 95.311 28.227 3.067 1.00 20.00 6 ATOM 575 CE1 PHE B 141 97.350 27.000 1.627 1.00 20.00 6 ATOM 576 CE2 PHE B 141 96.307 27.510 3.740 1.00 20.00 6 ATOM 577 CZ PHE B 141 97.328 26.895 3.018 1.00 20.00 6 ATOM 578 C PHE B 141 93.371 30.063 −1.181 1.00 20.00 6 ATOM 579 O PHE B 141 92.335 29.398 −1.114 1.00 20.00 8 ATOM 580 N PHE B 142 93.471 31.150 −1.934 1.00 20.00 7 ATOM 581 CA PHE B 142 92.337 31.625 −2.721 1.00 20.00 6 ATOM 582 CB PHE B 142 91.739 32.883 −2.082 1.00 20.00 6 ATOM 583 CG PHE B 142 91.048 32.628 −0.772 1.00 20.00 6 ATOM 584 CD1 PHE B 142 89.715 32.227 −0.740 1.00 20.00 6 ATOM 585 CD2 PHE B 142 91.741 32.747 0.429 1.00 20.00 6 ATOM 586 CE1 PHE B 142 89.080 31.944 0.472 1.00 20.00 6 ATOM 587 CE2 PHE B 142 91.116 32.465 1.647 1.00 20.00 6 ATOM 588 CZ PHE B 142 89.785 32.064 1.667 1.00 20.00 6 ATOM 589 C PHE B 142 92.758 31.945 −4.146 1.00 20.00 6 ATOM 590 O PHE B 142 93.865 32.429 −4.371 1.00 20.00 8 ATOM 591 N VAL B 143 91.883 31.653 −5.106 1.00 20.00 7 ATOM 592 CA VAL B 143 92.167 31.960 −6.504 1.00 20.00 6 ATOM 593 CB VAL B 143 91.009 31.513 −7.435 1.00 20.00 6 ATOM 594 CG1 VAL B 143 91.116 32.209 −8.795 1.00 20.00 6 ATOM 595 CG2 VAL B 143 91.061 30.000 −7.623 1.00 20.00 6 ATOM 596 C VAL B 143 92.301 33.469 −6.545 1.00 20.00 6 ATOM 597 O VAL B 143 91.505 34.179 −5.932 1.00 20.00 8 ATOM 598 N LYS B 144 93.312 33.957 −7.252 1.00 20.00 7 ATOM 599 CA LYS B 144 93.547 35.392 −7.340 1.00 20.00 6 ATOM 600 CB LYS B 144 95.051 35.689 −7.267 1.00 20.00 6 ATOM 601 CG LYS B 144 95.382 37.182 −7.318 1.00 20.00 6 ATOM 602 CD LYS B 144 96.881 37.441 −7.201 1.00 20.00 6 ATOM 603 CE LYS B 144 97.191 38.936 −7.298 1.00 20.00 6 ATOM 604 NZ LYS B 144 98.661 39.215 −7.246 1.00 20.00 7 ATOM 605 C LYS B 144 92.989 36.003 −8.614 1.00 20.00 6 ATOM 606 O LYS B 144 92.993 35.371 −9.675 1.00 20.00 8 ATOM 607 N LEU B 145 92.495 37.230 −8.490 1.00 20.00 7 ATOM 608 CA LEU B 145 91.968 37.975 −9.624 1.00 20.00 6 ATOM 609 CB LEU B 145 90.678 38.703 −9.234 1.00 20.00 6 ATOM 610 CG LEU B 145 89.938 39.486 −10.326 1.00 20.00 6 ATOM 611 CD1 LEU B 145 88.611 39.992 −9.782 1.00 20.00 6 ATOM 612 CD2 LEU B 145 90.791 40.652 −10.806 1.00 20.00 6 ATOM 613 C LEU B 145 93.059 38.984 −9.968 1.00 20.00 6 ATOM 614 O LEU B 145 93.291 39.940 −9.216 1.00 20.00 8 ATOM 615 N TYR B 146 93.735 38.770 −11.093 1.00 20.00 7 ATOM 616 CA TYR B 146 94.815 39.657 −11.517 1.00 20.00 6 ATOM 617 CB TYR B 146 95.821 38.904 −12.389 1.00 20.00 6 ATOM 618 CG TYR B 146 96.624 37.858 −11.661 1.00 20.00 6 ATOM 619 CD1 TYR B 146 96.139 36.559 −11.498 1.00 20.00 6 ATOM 620 CE1 TYR B 146 96.894 35.589 −10.836 1.00 20.00 6 ATOM 621 CD2 TYR B 146 97.878 38.165 −11.140 1.00 20.00 6 ATOM 622 CE2 TYR B 146 98.639 37.208 −10.476 1.00 20.00 6 ATOM 623 CZ TYR B 146 98.144 35.925 −10.331 1.00 20.00 6 ATOM 624 OH TYR B 146 98.920 34.981 −9.706 1.00 20.00 8 ATOM 625 C TYR B 146 94.357 40.884 −12.293 1.00 20.00 6 ATOM 626 O TYR B 146 94.933 41.963 −12.160 1.00 20.00 8 ATOM 627 N PHE B 147 93.326 40.722 −13.110 1.00 20.00 7 ATOM 628 CA PHE B 147 92.855 41.832 −13.923 1.00 20.00 6 ATOM 629 CB PHE B 147 93.823 42.044 −15.092 1.00 20.00 6 ATOM 630 CG PHE B 147 94.027 40.809 −15.945 1.00 20.00 6 ATOM 631 CD1 PHE B 147 93.049 40.397 −16.850 1.00 20.00 6 ATOM 632 CD2 PHE B 147 95.188 40.047 −15.822 1.00 20.00 6 ATOM 633 CE1 PHE B 147 93.221 39.247 −17.617 1.00 20.00 6 ATOM 634 CE2 PHE B 147 95.372 38.893 −16.585 1.00 20.00 6 ATOM 635 CZ PHE B 147 94.388 38.490 −17.485 1.00 20.00 6 ATOM 636 C PHE B 147 91.473 41.566 −14.480 1.00 20.00 6 ATOM 637 O PHE B 147 90.972 40.442 −14.423 1.00 20.00 8 ATOM 638 N THR B 148 90.865 42.616 −15.021 1.00 20.00 7 ATOM 639 CA THR B 148 89.560 42.509 −15.643 1.00 20.00 6 ATOM 640 CB THR B 148 88.402 42.889 −14.678 1.00 20.00 6 ATOM 641 OG1 THR B 148 88.492 44.275 −14.338 1.00 20.00 8 ATOM 642 CG2 THR B 148 88.460 42.057 −13.403 1.00 20.00 6 ATOM 643 C THR B 148 89.532 43.469 −16.821 1.00 20.00 6 ATOM 644 O THR B 148 90.281 44.448 −16.866 1.00 20.00 8 ATOM 645 N PHE B 149 88.685 43.161 −17.791 1.00 20.00 7 ATOM 646 CA PHE B 149 88.508 44.011 −18.948 1.00 20.00 6 ATOM 647 CB PHE B 149 89.750 44.013 −19.864 1.00 20.00 6 ATOM 648 CG PHE B 149 90.133 42.664 −20.419 1.00 20.00 6 ATOM 649 CD1 PHE B 149 89.552 42.182 −21.587 1.00 20.00 6 ATOM 650 CD2 PHE B 149 91.122 41.903 −19.802 1.00 20.00 6 ATOM 651 CE1 PHE B 149 89.953 40.965 −22.142 1.00 20.00 6 ATOM 652 CE2 PHE B 149 91.532 40.681 −20.345 1.00 20.00 6 ATOM 653 CZ PHE B 149 90.948 40.213 −21.517 1.00 20.00 6 ATOM 654 C PHE B 149 87.271 43.498 −19.649 1.00 20.00 6 ATOM 655 O PHE B 149 86.714 42.474 −19.251 1.00 20.00 8 ATOM 656 N GLN B 150 86.812 44.221 −20.657 1.00 20.00 7 ATOM 657 CA GLN B 150 85.619 43.807 −21.372 1.00 20.00 6 ATOM 658 CB GLN B 150 84.358 44.260 −20.614 1.00 20.00 6 ATOM 659 CG GLN B 150 84.302 45.761 −20.289 1.00 20.00 6 ATOM 660 CD GLN B 150 83.011 46.172 −19.567 1.00 20.00 6 ATOM 661 OE1 GLN B 150 81.970 46.385 −20.196 1.00 20.00 8 ATOM 662 NE2 GLN B 150 83.078 46.273 −18.240 1.00 20.00 7 ATOM 663 C GLN B 150 85.598 44.400 −22.760 1.00 20.00 6 ATOM 664 O GLN B 150 86.281 45.387 −23.033 1.00 20.00 8 ATOM 665 N ASP B 151 84.846 43.766 −23.649 1.00 20.00 7 ATOM 666 CA ASP B 151 84.683 44.296 −24.992 1.00 20.00 6 ATOM 667 CB ASP B 151 85.160 43.312 −26.074 1.00 20.00 6 ATOM 668 CG ASP B 151 84.558 41.934 −25.939 1.00 20.00 6 ATOM 669 OD1 ASP B 151 83.425 41.812 −25.436 1.00 20.00 8 ATOM 670 OD2 ASP B 151 85.227 40.963 −26.365 1.00 20.00 8 ATOM 671 C ASP B 151 83.188 44.573 −25.095 1.00 20.00 6 ATOM 672 O ASP B 151 82.501 44.610 −24.069 1.00 20.00 8 ATOM 673 N ASP B 152 82.669 44.758 −26.301 1.00 20.00 7 ATOM 674 CA ASP B 152 81.251 45.062 −26.437 1.00 20.00 6 ATOM 675 CB ASP B 152 80.907 45.346 −27.901 1.00 20.00 6 ATOM 676 CG ASP B 152 81.616 46.574 −28.432 1.00 20.00 6 ATOM 677 OD1 ASP B 152 81.748 47.555 −27.666 1.00 20.00 8 ATOM 678 OD2 ASP B 152 82.030 46.563 −29.613 1.00 20.00 8 ATOM 679 C ASP B 152 80.285 44.020 −25.888 1.00 20.00 6 ATOM 680 O ASP B 152 79.229 44.367 −25.357 1.00 20.00 8 ATOM 681 N GLU B 153 80.641 42.747 −25.982 1.00 20.00 7 ATOM 682 CA GLU B 153 79.727 41.711 −25.521 1.00 20.00 6 ATOM 683 CB GLU B 153 79.516 40.685 −26.641 1.00 20.00 6 ATOM 684 CG GLU B 153 79.577 41.260 −28.058 1.00 20.00 6 ATOM 685 CD GLU B 153 81.006 41.472 −28.550 1.00 20.00 6 ATOM 686 OE1 GLU B 153 81.765 40.480 −28.635 1.00 20.00 8 ATOM 687 OE2 GLU B 153 81.374 42.627 −28.854 1.00 20.00 8 ATOM 688 C GLU B 153 80.102 40.960 −24.247 1.00 20.00 6 ATOM 689 O GLU B 153 79.222 40.473 −23.535 1.00 20.00 8 ATOM 690 N LYS B 154 81.393 40.869 −23.944 1.00 20.00 7 ATOM 691 CA LYS B 154 81.818 40.091 −22.787 1.00 20.00 6 ATOM 692 CB LYS B 154 82.549 38.830 −23.273 1.00 20.00 6 ATOM 693 CG LYS B 154 81.785 37.978 −24.278 1.00 20.00 6 ATOM 694 CD LYS B 154 82.727 37.028 −25.021 1.00 20.00 6 ATOM 695 CE LYS B 154 81.968 36.086 −25.952 1.00 20.00 6 ATOM 696 NZ LYS B 154 82.894 35.300 −26.826 1.00 20.00 7 ATOM 697 C LYS B 154 82.709 40.767 −21.756 1.00 20.00 6 ATOM 698 O LYS B 154 83.412 41.740 −22.048 1.00 20.00 8 ATOM 699 N LEU B 155 82.677 40.202 −20.551 1.00 20.00 7 ATOM 700 CA LEU B 155 83.501 40.638 −19.428 1.00 20.00 6 ATOM 701 CB LEU B 155 82.700 40.651 −18.127 1.00 20.00 6 ATOM 702 CG LEU B 155 81.451 41.521 −18.004 1.00 20.00 6 ATOM 703 CD1 LEU B 155 80.805 41.273 −16.645 1.00 20.00 6 ATOM 704 CD2 LEU B 155 81.831 42.983 −18.152 1.00 20.00 6 ATOM 705 C LEU B 155 84.578 39.559 −19.302 1.00 20.00 6 ATOM 706 O LEU B 155 84.288 38.379 −19.495 1.00 20.00 8 ATOM 707 N TYR B 156 85.802 39.956 −18.966 1.00 20.00 7 ATOM 708 CA TYR B 156 86.893 38.998 −18.809 1.00 20.00 6 ATOM 709 CB TYR B 156 87.953 39.189 −19.904 1.00 20.00 6 ATOM 710 CG TYR B 156 87.450 39.053 −21.324 1.00 20.00 6 ATOM 711 CD1 TYR B 156 86.688 40.061 −21.920 1.00 20.00 6 ATOM 712 CE1 TYR B 156 86.233 39.938 −23.235 1.00 20.00 6 ATOM 713 CD2 TYR B 156 87.741 37.917 −22.077 1.00 20.00 6 ATOM 714 CE2 TYR B 156 87.288 37.782 −23.387 1.00 20.00 6 ATOM 715 CZ TYR B 156 86.538 38.794 −23.958 1.00 20.00 6 ATOM 716 OH TYR B 156 86.087 38.656 −25.246 1.00 20.00 8 ATOM 717 C TYR B 156 87.566 39.182 −17.447 1.00 20.00 6 ATOM 718 O TYR B 156 87.977 40.291 −17.110 1.00 20.00 8 ATOM 719 N PHE B 157 87.657 38.104 −16.667 1.00 20.00 7 ATOM 720 CA PHE B 157 88.325 38.152 −15.367 1.00 20.00 6 ATOM 721 CB PHE B 157 87.448 37.575 −14.246 1.00 20.00 6 ATOM 722 CG PHE B 157 86.194 38.360 −13.968 1.00 20.00 6 ATOM 723 CD1 PHE B 157 85.986 39.614 −14.535 1.00 20.00 6 ATOM 724 CD2 PHE B 157 85.206 37.828 −13.143 1.00 20.00 6 ATOM 725 CE1 PHE B 157 84.808 40.324 −14.290 1.00 20.00 6 ATOM 726 CE2 PHE B 157 84.025 38.532 −12.893 1.00 20.00 6 ATOM 727 CZ PHE B 157 83.829 39.782 −13.470 1.00 20.00 6 ATOM 728 C PHE B 157 89.579 37.295 −15.471 1.00 20.00 6 ATOM 729 O PHE B 157 89.492 36.105 −15.765 1.00 20.00 8 ATOM 730 N GLY B 158 90.742 37.893 −15.231 1.00 20.00 7 ATOM 731 CA GLY B 158 91.985 37.146 −15.303 1.00 20.00 6 ATOM 732 C GLY B 158 92.254 36.512 −13.955 1.00 20.00 6 ATOM 733 O GLY B 158 92.575 37.211 −12.996 1.00 20.00 8 ATOM 734 N LEU B 159 92.137 35.191 13.886 1.00 20.00 7 ATOM 735 CA LEU B 159 92.330 34.466 −12.634 1.00 20.00 6 ATOM 736 CB LEU B 159 91.116 33.580 −12.358 1.00 20.00 6 ATOM 737 CG LEU B 159 89.724 34.208 −12.490 1.00 20.00 6 ATOM 738 CD1 LEU B 159 88.670 33.111 −12.398 1.00 20.00 6 ATOM 739 CD2 LEU B 159 89.513 35.246 −11.404 1.00 20.00 6 ATOM 740 C LEU B 159 93.562 33.582 −12.643 1.00 20.00 6 ATOM 741 O LEU B 159 94.061 33.204 −13.698 1.00 20.00 8 ATOM 742 N SER B 160 94.046 33.237 −11.457 1.00 20.00 7 ATOM 743 CA SER B 160 95.192 32.356 −11.377 1.00 20.00 6 ATOM 744 CB SER B 160 95.665 32.206 −9.926 1.00 20.00 6 ATOM 745 OG SER B 160 94.591 31.973 '19.042 1.00 20.00 8 ATOM 746 C SER B 160 94.754 31.012 −11.951 1.00 20.00 6 ATOM 747 O SER B 160 93.598 30.605 −11.813 1.00 20.00 8 ATOM 748 N TYR B 161 95.674 30.339 −12.625 1.00 20.00 7 ATOM 749 CA TYR B 161 95.381 29.050 −13.231 1.00 20.00 6 ATOM 750 CB TYR B 161 96.170 28.924 −14.543 1.00 20.00 6 ATOM 751 CG TYR B 161 96.128 27.564 −15.209 1.00 20.00 6 ATOM 752 CD1 TYR B 161 94.968 26.787 −15.193 1.00 20.00 6 ATOM 753 CE1 TYR B 161 94.915 25.554 −15.846 1.00 20.00 6 ATOM 754 CD2 TYR B 161 97.240 27.073 −15.895 1.00 20.00 6 ATOM 755 CE2 TYR B 161 97.198 25.841 −16.553 1.00 20.00 6 ATOM 756 CZ TYR B 161 96.033 25.088 −16.523 1.00 20.00 6 ATOM 757 OH TYR B 161 95.983 23.877 −17.173 1.00 20.00 8 ATOM 758 C TYR B 161 95.724 27.905 −12.277 1.00 20.00 6 ATOM 759 O TYR B 161 96.897 27.598 −12.065 1.00 20.00 8 ATOM 760 N ALA B 162 94.696 27.288 −11.697 1.00 20.00 7 ATOM 761 CA ALA B 162 94.893 26.166 −10.776 1.00 20.00 6 ATOM 762 CB ALA B 162 93.666 25.995 −9.873 1.00 20.00 6 ATOM 763 C ALA B 162 95.100 24.924 −11.637 1.00 20.00 6 ATOM 764 O ALA B 162 94.146 24.251 −12.015 1.00 20.00 8 ATOM 765 N LYS B 163 96.361 24.626 −11.930 1.00 20.00 7 ATOM 766 CA LYS B 163 96.722 23.506 −12.795 1.00 20.00 6 ATOM 767 CB LYS B 163 98.247 23.416 −12.912 1.00 20.00 6 ATOM 768 CG LYS B 163 98.904 24.711 −13.360 1.00 20.00 6 ATOM 769 CD LYS B 163 100.405 24.539 13.554 1.00 20.00 6 ATOM 770 CE LYS B 163 101.102 25.885 −13.690 1.00 20.00 6 ATOM 771 NZ LYS B 163 100.976 26.701 −12.445 1.00 20.00 7 ATOM 772 C LYS B 163 96.170 22.123 12.464 1.00 20.00 6 ATOM 773 O LYS B 163 95.823 21.370 −13.369 1.00 20.00 8 ATOM 774 N ASN B 164 96.076 21.775 −11.186 1.00 20.00 7 ATOM 775 CA ASN B 164 95.594 20.449 −10.842 1.00 20.00 6 ATOM 776 CB ASN B 164 96.339 19.944 −9.610 1.00 20.00 6 ATOM 777 CG ASN B 164 97.766 19.529 −9.943 1.00 20.00 6 ATOM 778 OD1 ASN B 164 97.992 18.776 −10.892 1.00 20.00 8 ATOM 779 ND2 ASN B 164 98.730 20.014 −9.171 1.00 20.00 7 ATOM 780 C ASN B 164 94.084 20.246 −10.706 1.00 20.00 6 ATOM 781 O ASN B 164 93.630 19.183 −10.286 1.00 20.00 8 ATOM 782 N GLY B 165 93.309 21.257 −11.080 1.00 20.00 7 ATOM 783 CA GLY B 165 91.863 21.127 −11.039 1.00 20.00 6 ATOM 784 C GLY B 165 91.159 21.088 9.694 1.00 20.00 6 ATOM 785 O GLY B 165 91.663 21.598 8.698 1.00 20.00 8 ATOM 786 N GLU B 166 89.986 20.461 −9.689 1.00 20.00 7 ATOM 787 CA GLU B 166 89.126 20.344 −8.513 1.00 20.00 6 ATOM 788 CB GLU B 166 87.683 20.079 −8.962 1.00 20.00 6 ATOM 789 CG GLU B 166 86.992 21.255 −9.646 1.00 20.00 6 ATOM 790 CD GLU B 166 85.709 20.837 −10.358 1.00 20.00 6 ATOM 791 OE1 GLU B 166 85.137 19.794 −9.986 1.00 20.00 8 ATOM 792 OE2 GLU B 166 85.263 21.556 −11.279 1.00 20.00 8 ATOM 793 C GLU B 166 89.520 19.270 −7.506 1.00 20.00 6 ATOM 794 O GLU B 166 89.952 18.184 −7.874 1.00 20.00 8 ATOM 795 N LEU B 167 89.344 19.579 −6.226 1.00 20.00 7 ATOM 796 CA LEU B 167 89.651 18.626 −5.168 1.00 20.00 6 ATOM 797 CB LEU B 167 89.395 19.269 −3.802 1.00 20.00 6 ATOM 798 CG LEU B 167 89.408 18.363 −2.569 1.00 20.00 6 ATOM 799 CD1 LEU B 167 90.769 17.703 −2.412 1.00 20.00 6 ATOM 800 CD2 LEU B 167 89.065 19.193 −1.338 1.00 20.00 6 ATOM 801 C LEU B 167 88.757 17.394 −5.346 1.00 20.00 6 ATOM 802 O LEU B 167 89.124 16.283 −4.968 1.00 20.00 8 ATOM 803 N LEU B 168 87.580 17.600 −5.927 1.00 20.00 7 ATOM 804 CA LEU B 168 86.647 16.500 −6.153 1.00 20.00 6 ATOM 805 CB LEU B 168 85.364 17.014 −6.809 1.00 20.00 6 ATOM 806 CG LEU B 168 84.292 15.977 −7.168 1.00 20.00 6 ATOM 807 CD1 LEU B 168 83.883 15.186 −5.929 1.00 20.00 6 ATOM 808 CD2 LEU B 168 83.083 16.687 −7.756 1.00 20.00 6 ATOM 809 C LEU B 168 87.290 15.440 −7.046 1.00 20.00 6 ATOM 810 O LEU B 168 87.091 14.243 −6.845 1.00 20.00 8 ATOM 811 N LYS B 169 88.068 15.888 −8.027 1.00 20.00 7 ATOM 812 CA LYS B 169 88.727 14.967 −8.941 1.00 20.00 6 ATOM 813 CB LYS B 169 89.610 15.729 −9.930 1.00 20.00 6 ATOM 814 CG LYS B 169 90.379 14.818 −10.882 1.00 20.00 6 ATOM 815 CD LYS B 169 91.226 15.603 −11.877 1.00 20.00 6 ATOM 816 CE LYS B 169 92.373 16.328 −11.192 1.00 20.00 6 ATOM 817 NZ LYS B 169 93.253 17.021 −12.173 1.00 20.00 7 ATOM 818 C LYS B 169 89.574 13.949 −8.193 1.00 20.00 6 ATOM 819 O LYS B 169 89.543 12.758 −8.504 1.00 20.00 8 ATOM 820 N TYR B 170 90.334 14.417 −7.207 1.00 20.00 7 ATOM 821 CA TYR B 170 91.197 13.527 −6.441 1.00 20.00 6 ATOM 822 CB TYR B 170 92.243 14.346 −5.682 1.00 20.00 6 ATOM 823 CG TYR B 170 93.217 15.010 −6.624 1.00 20.00 6 ATOM 824 CD1 TYR B 170 94.347 14.331 −7.085 1.00 20.00 6 ATOM 825 CE1 TYR B 170 95.195 14.900 −8.036 1.00 20.00 6 ATOM 826 CD2 TYR B 170 92.963 16.282 −7.133 1.00 20.00 6 ATOM 827 CE2 TYR B 170 93.801 16.861 −8.083 1.00 20.00 6 ATOM 828 CZ TYR B 170 94.913 16.164 −8.532 1.00 20.00 6 ATOM 829 OH TYR B 170 95.727 16.727 −9.493 1.00 20.00 8 ATOM 830 C TYR B 170 90.419 12.622 −5.499 1.00 20.00 6 ATOM 831 O TYR B 170 90.834 11.494 −5.233 1.00 20.00 8 ATOM 832 N ILE B 171 89.287 13.098 −4.993 1.00 20.00 7 ATOM 833 CA ILE B 171 88.488 12.262 −4.112 1.00 20.00 6 ATOM 834 CB ILE B 171 87.278 13.028 −3.538 1.00 20.00 6 ATOM 835 CG2 ILE B 171 86.367 12.065 −2.791 1.00 20.00 6 ATOM 836 CG1 ILE B 171 87.764 14.141 −2.603 1.00 20.00 6 ATOM 837 CD1 ILE B 171 86.652 14.990 −2.019 1.00 20.00 6 ATOM 838 C ILE B 171 87.994 11.066 −4.931 1.00 20.00 6 ATOM 839 O ILE B 171 88.030 9.925 −4.468 1.00 20.00 8 ATOM 840 N ARG B 172 87.550 11.331 −6.156 1.00 20.00 7 ATOM 841 CA ARG B 172 87.061 10.273 −7.031 1.00 20.00 6 ATOM 842 CB ARG B 172 86.359 10.861 −8.259 1.00 20.00 6 ATOM 843 CG ARG B 172 85.094 11.658 −7.963 1.00 20.00 6 ATOM 844 CD ARG B 172 84.352 11.981 −9.259 1.00 20.00 6 ATOM 845 NE ARG B 172 83.187 12.843 −9.063 1.00 20.00 7 ATOM 846 CZ ARG B 172 82.192 12.589 −8.217 1.00 20.00 6 ATOM 847 NH1 ARG B 172 82.209 11.491 −7.469 1.00 20.00 7 ATOM 848 NH2 ARG B 172 81.168 13.428 −8.127 1.00 20.00 7 ATOM 849 C ARG B 172 88.202 9.378 −7.497 1.00 20.00 6 ATOM 850 O ARG B 172 88.050 8.160 −7.587 1.00 20.00 8 ATOM 851 N LYS B 173 89.348 9.985 −7.783 1.00 20.00 7 ATOM 852 CA LYS B 173 90.509 9.244 −8.256 1.00 20.00 6 ATOM 853 CB LYS B 173 91.647 10.206 −8.603 1.00 20.00 6 ATOM 854 CG LYS B 173 92.930 9.511 −9.045 1.00 20.00 6 ATOM 855 CD LYS B 173 94.081 10.496 −9.222 1.00 20.00 6 ATOM 856 CE LYS B 173 93.862 11.432 −10.406 1.00 20.00 6 ATOM 857 NZ LYS B 173 93.858 10.711 −11.715 1.00 20.00 7 ATOM 858 C LYS B 173 91.025 8.191 −7.280 1.00 20.00 6 ATOM 859 O LYS B 173 91.274 7.055 −7.674 1.00 20.00 8 ATOM 860 N ILE B 174 91.192 8.554 −6.012 1.00 20.00 7 ATOM 861 CA ILE B 174 91.710 7.593 −5.042 1.00 20.00 6 ATOM 862 CB ILE B 174 92.884 8.191 −4.223 1.00 20.00 6 ATOM 863 CG2 ILE B 174 93.970 8.701 −5.166 1.00 20.00 6 ATOM 864 CG1 ILE B 174 92.394 9.337 −3.343 1.00 20.00 6 ATOM 865 CD1 ILE B 174 93.480 9.916 −2.457 1.00 20.00 6 ATOM 866 C ILE B 174 90.674 7.030 −4.074 1.00 20.00 6 ATOM 867 O ILE B 174 91.025 6.296 −3.151 1.00 20.00 8 ATOM 868 N GLY B 175 89.405 7.367 −4.283 1.00 20.00 7 ATOM 869 CA GLY B 175 88.359 6.855 −3.413 1.00 20.00 6 ATOM 870 C GLY B 175 88.160 7.650 −2.138 1.00 20.00 6 ATOM 871 O GLY B 175 87.083 8.198 −1.905 1.00 20.00 8 ATOM 872 N SER B 176 89.192 7.701 −1.304 1.00 20.00 7 ATOM 873 CA SER B 176 89.140 8.447 −0.053 1.00 20.00 6 ATOM 874 CB SER B 176 88.395 7.653 1.026 1.00 20.00 6 ATOM 875 OG SER B 176 89.150 6.543 1.472 1.00 20.00 8 ATOM 876 C SER B 176 90.565 8.742 0.401 1.00 20.00 6 ATOM 877 O SER B 176 91.506 8.049 0.009 1.00 20.00 8 ATOM 878 N PHE B 177 90.718 9.769 1.228 1.00 20.00 7 ATOM 879 CA PHE B 177 92.029 10.184 1.722 1.00 20.00 6 ATOM 880 CB PHE B 177 92.028 11.694 1.990 1.00 20.00 6 ATOM 881 CG PHE B 177 92.002 12.546 0.747 1.00 20.00 6 ATOM 882 CD1 PHE B 177 91.484 12.060 −0.449 1.00 20.00 6 ATOM 883 CD2 PHE B 177 92.481 13.855 0.787 1.00 20.00 6 ATOM 884 CE1 PHE B 177 91.443 12.860 −1.585 1.00 20.00 6 ATOM 885 CE2 PHE B 177 92.444 14.665 −0.343 1.00 20.00 6 ATOM 886 CZ PHE B 177 91.925 14.168 −1.532 1.00 20.00 6 ATOM 887 C PHE B 177 92.427 9.475 3.009 1.00 20.00 6 ATOM 888 O PHE B 177 91.582 9.223 3.872 1.00 20.00 8 ATOM 889 N ASP B 178 93.711 9.152 3.147 1.00 20.00 7 ATOM 890 CA ASP B 178 94.155 8.529 4.385 1.00 20.00 6 ATOM 891 CB ASP B 178 95.581 7.972 4.267 1.00 20.00 6 ATOM 892 CG ASP B 178 96.594 9.018 3.845 1.00 20.00 6 ATOM 893 OD1 ASP B 178 96.392 10.214 4.139 1.00 20.00 8 ATOM 894 OD2 ASP B 178 97.612 8.634 3.230 1.00 20.00 8 ATOM 895 C ASP B 178 94.092 9.640 5.436 1.00 20.00 6 ATOM 896 O ASP B 178 93.736 10.778 5.117 1.00 20.00 8 ATOM 897 N GLU B 179 94.443 9.324 6.677 1.00 20.00 7 ATOM 898 CA GLU B 179 94.380 10.311 7.744 1.00 20.00 6 ATOM 899 CB GLU B 179 94.623 9.637 9.096 1.00 20.00 6 ATOM 900 CG GLU B 179 94.747 10.611 10.255 1.00 20.00 6 ATOM 901 CD GLU B 179 94.331 9.994 11.574 1.00 20.00 6 ATOM 902 OE1 GLU B 179 94.589 8.789 11.770 1.00 20.00 8 ATOM 903 OE2 GLU B 179 93.753 10.717 12.416 1.00 20.00 8 ATOM 904 C GLU B 179 95.320 11.501 7.575 1.00 20.00 6 ATOM 905 O GLU B 179 94.948 12.636 7.881 1.00 20.00 8 ATOM 906 N THR B 180 96.528 11.246 7.086 1.00 20.00 7 ATOM 907 CA THR B 180 97.509 12.308 6.886 1.00 20.00 6 ATOM 908 CB THR B 180 98.866 11.720 6.445 1.00 20.00 6 ATOM 909 OG1 THR B 180 99.349 10.842 7.466 1.00 20.00 8 ATOM 910 CG2 THR B 180 99.888 12.825 6.213 1.00 20.00 6 ATOM 911 C THR B 180 97.040 13.331 5.849 1.00 20.00 6 ATOM 912 O THR B 180 97.136 14.542 6.069 1.00 20.00 8 ATOM 913 N CYS B 181 96.534 12.845 4.721 1.00 20.00 7 ATOM 914 CA CYS B 181 96.057 13.733 3.666 1.00 20.00 6 ATOM 915 CB CYS B 181 95.836 12.945 2.375 1.00 20.00 6 ATOM 916 SG CYS B 181 97.372 12.255 1.685 1.00 20.00 16 ATOM 917 C CYS B 181 94.775 14.449 4.079 1.00 20.00 6 ATOM 918 O CYS B 181 94.570 15.615 3.733 1.00 20.00 8 ATOM 919 N THR B 182 93.914 13.755 4.820 1.00 20.00 7 ATOM 920 CA THR B 182 92.669 14.356 5.286 1.00 20.00 6 ATOM 921 CB THR B 182 91.812 13.354 6.103 1.00 20.00 6 ATOM 922 OG1 THR B 182 91.372 12.283 5.259 1.00 20.00 8 ATOM 923 CG2 THR B 182 90.600 14.054 6.690 1.00 20.00 6 ATOM 924 C THR B 182 93.014 15.535 6.196 1.00 20.00 6 ATOM 925 O THR B 182 92.515 16.649 6.019 1.00 20.00 8 ATOM 926 N ARG B 183 93.873 15.273 7.175 1.00 20.00 7 ATOM 927 CA ARG B 183 94.299 16.293 8.121 1.00 20.00 6 ATOM 928 CB ARG B 183 95.311 15.707 9.109 1.00 20.00 6 ATOM 929 CG ARG B 183 95.957 16.744 10.012 1.00 20.00 6 ATOM 930 CD ARG B 183 96.886 16.116 11.050 1.00 20.00 6 ATOM 931 NE ARG B 183 96.167 15.220 11.949 1.00 20.00 7 ATOM 932 CZ ARG B 183 96.098 13.900 11.804 1.00 20.00 6 ATOM 933 NH1 ARG B 183 96.717 13.306 10.791 1.00 20.00 7 ATOM 934 NH2 ARG B 183 95.389 13.176 12.664 1.00 20.00 7 ATOM 935 C ARG B 183 94.923 17.505 7.427 1.00 20.00 6 ATOM 936 O ARG B 183 94.545 18.646 7.698 1.00 20.00 8 ATOM 937 N PHE B 184 95.877 17.264 6.534 1.00 20.00 7 ATOM 938 CA PHE B 184 96.539 18.367 5.847 1.00 20.00 6 ATOM 939 CB PHE B 184 97.610 17.847 4.889 1.00 20.00 6 ATOM 940 CG PHE B 184 98.387 18.943 4.223 1.00 20.00 6 ATOM 941 CD1 PHE B 184 99.451 19.555 4.879 1.00 20.00 6 ATOM 942 CD2 PHE B 184 98.009 19.415 2.975 1.00 20.00 6 ATOM 943 CE1 PHE B 184 100.125 20.627 4.301 1.00 20.00 6 ATOM 944 CE2 PHE B 184 98.676 20.491 2.388 1.00 20.00 6 ATOM 945 CZ PHE B 184 99.735 21.097 3.053 1.00 20.00 6 ATOM 946 C PHE B 184 95.580 19.267 5.066 1.00 20.00 6 ATOM 947 O PHE B 184 95.567 20.481 5.255 1.00 20.00 8 ATOM 948 N TYR B 185 94.784 18.679 4.181 1.00 20.00 7 ATOM 949 CA TYR B 185 93.854 19.471 3.390 1.00 20.00 6 ATOM 950 CB TYR B 185 93.305 18.634 2.236 1.00 20.00 6 ATOM 951 CG TYR B 185 94.337 18.504 1.140 1.00 20.00 6 ATOM 952 CD1 TYR B 185 94.611 19.580 0.293 1.00 20.00 6 ATOM 953 CE1 TYR B 185 95.637 19.516 −0.643 1.00 20.00 6 ATOM 954 CD2 TYR B 185 95.118 17.352 1.017 1.00 20.00 6 ATOM 955 CE2 TYR B 185 96.152 17.282 0.081 1.00 20.00 6 ATOM 956 CZ TYR B 185 96.405 18.367 −0.742 1.00 20.00 6 ATOM 957 OH TYR B 185 97.436 18.314 −1.657 1.00 20.00 8 ATOM 958 C TYR B 185 92.738 20.098 4.208 1.00 20.00 6 ATOM 959 O TYR B 185 92.286 21.195 3.891 1.00 20.00 8 ATOM 960 N THR B 186 92.303 19.422 5.267 1.00 20.00 7 ATOM 961 CA THR B 186 91.265 19.987 6.122 1.00 20.00 6 ATOM 962 CB THR B 186 90.799 18.996 7.219 1.00 20.00 6 ATOM 96 OG1 THR B 186 90.193 17.846 6.606 1.00 20.00 8 ATOM 964 CG2 THR B 186 89.774 19.671 8.144 1.00 20.00 6 ATOM 965 C THR B 186 91.858 21.218 6.805 1.00 20.00 6 ATOM 966 O THR B 186 91.188 22.242 6.948 1.00 20.00 8 ATOM 967 N ALA B 187 93.120 21.115 7.222 1.00 20.00 7 ATOM 968 CA ALA B 187 93.787 22.234 7.882 1.00 20.00 6 ATOM 969 CB ALA B 187 95.184 21.817 8.349 1.00 20.00 6 ATOM 970 C ALA B 187 93.879 23.449 6.946 1.00 20.00 6 ATOM 971 O ALA B 187 93.654 24.585 7.372 1.00 20.00 8 ATOM 972 N GLU B 188 94.205 23.222 5.674 1.00 20.00 7 ATOM 973 CA GLU B 188 94.292 24.343 4.740 1.00 20.00 6 ATOM 974 CB GLU B 188 94.843 23.898 3.376 1.00 20.00 6 ATOM 975 CG GLU B 188 96.285 23.391 3.407 1.00 20.00 6 ATOM 976 CD GLU B 188 97.030 23.639 2.104 1.00 20.00 6 ATOM 977 OE1 GLU B 188 96.407 23.537 1.024 1.00 20.00 8 ATOM 978 OE2 GLU B 188 98.247 23.932 2.156 1.00 20.00 8 ATOM 979 C GLU B 188 92.912 24.977 4.561 1.00 20.00 6 ATOM 980 O GLU B 188 92.782 26.196 4.533 1.00 20.00 8 ATOM 981 N ILE B 189 91.875 24.152 4.451 1.00 20.00 7 ATOM 982 CA ILE B 189 90.530 24.693 4.284 1.00 20.00 6 ATOM 983 CB ILE B 189 89.495 23.566 4.064 1.00 20.00 6 ATOM 984 CG2 ILE B 189 88.094 24.157 3.947 1.00 20.00 6 ATOM 985 CG1 ILE B 189 89.855 22.773 2.796 1.00 20.00 6 ATOM 986 CD1 ILE B 189 89.058 21.488 2.616 1.00 20.00 6 ATOM 987 C ILE B 189 90.152 25.517 5.519 1.00 20.00 6 ATOM 988 O ILE B 189 89.634 26.630 5.396 1.00 20.00 8 ATOM 989 N VAL B 190 90.412 24.971 6.707 1.00 20.00 7 ATOM 990 CA VAL B 190 90.116 25.674 7.957 1.00 20.00 6 ATOM 991 CB VAL B 190 90.557 24.842 9.186 1.00 20.00 6 ATOM 992 CG1 VAL B 190 90.540 25.717 10.451 1.00 20.00 6 ATOM 993 CG2 VAL B 190 89.643 23.641 9.358 1.00 20.00 6 ATOM 994 C VAL B 190 90.865 27.012 7.984 1.00 20.00 6 ATOM 995 O VAL B 190 90.311 28.039 8.375 1.00 20.00 8 ATOM 996 N SER B 191 92.125 26.997 7.557 1.00 20.00 7 ATOM 997 CA SER B 191 92.934 28.218 7.546 1.00 20.00 6 ATOM 998 CB SER B 191 94.378 27.888 7.166 1.00 20.00 6 ATOM 999 OG SER B 191 95.220 29.007 7.363 1.00 20.00 8 ATOM 1000 C SER B 191 92.361 29.240 6.566 1.00 20.00 6 ATOM 1001 O SER B 191 92.351 30.444 6.838 1.00 20.00 8 ATOM 1002 N ALA B 192 91.882 28.754 5.425 1.00 20.00 7 ATOM 1003 CA ALA B 192 91.306 29.634 4.417 1.00 20.00 6 ATOM 1004 CB ALA B 192 91.006 28.850 3.141 1.00 20.00 6 ATOM 1005 C ALA B 192 90.029 30.256 4.970 1.00 20.00 6 ATOM 1006 O ALA B 192 89.799 31.458 4.822 1.00 20.00 8 ATOM 1007 N LEU B 193 89.203 29.439 5.621 1.00 20.00 7 ATOM 1008 CA LEU B 193 87.957 29.941 6.192 1.00 20.00 6 ATOM 1009 CB LEU B 193 87.101 28.783 6.725 1.00 20.00 6 ATOM 1010 CG LEU B 193 86.447 27.898 5.650 1.00 20.00 6 ATOM 1011 CD1 LEU B 193 85.645 26.771 6.315 1.00 20.00 6 ATOM 1012 CD2 LEU B 193 85.530 28.752 4.780 1.00 20.00 6 ATOM 1013 C LEU B 193 88.215 30.959 7.299 1.00 20.00 6 ATOM 1014 O LEU B 193 87.474 31.935 7.435 1.00 20.00 8 ATOM 1015 N GLU B 194 89.254 30.738 8.100 1.00 20.00 7 ATOM 1016 CA GLU B 194 89.562 31.699 9.157 1.00 20.00 6 ATOM 1017 CB GLU B 194 90.773 31.257 9.982 1.00 20.00 6 ATOM 1018 CG GLU B 194 91.288 32.353 10.914 1.00 20.00 6 ATOM 1019 CD GLU B 194 92.381 31.878 11.855 1.00 20.00 6 ATOM 1020 OE1 GLU B 194 93.246 31.090 11.420 1.00 20.00 8 ATOM 1021 OE2 GLU B 194 92.376 32.312 13.031 1.00 20.00 8 ATOM 1022 C GLU B 194 89.847 33.053 8.511 1.00 20.00 6 ATOM 1023 O GLU B 194 89.375 34.083 8.972 1.00 20.00 8 ATOM 1024 N TYR B 195 90.608 33.046 7.426 1.00 20.00 7 ATOM 1025 CA TYR B 195 90.928 34.294 6.743 1.00 20.00 6 ATOM 1026 CB TYR B 195 91.919 34.043 5.613 1.00 20.00 6 ATOM 1027 CG TYR B 195 92.193 35.271 4.774 1.00 20.00 6 ATOM 1028 CD1 TYR B 195 93.098 36.244 5.202 1.00 20.00 6 ATOM 1029 CE1 TYR B 195 93.356 37.382 4.429 1.00 20.00 6 ATOM 1030 CD2 TYR B 195 91.545 35.461 3.553 1.00 20.00 6 ATOM 1031 CE2 TYR B 195 91.794 36.591 2.775 1.00 20.00 6 ATOM 1032 CZ TYR B 195 92.701 37.545 3.219 1.00 20.00 6 ATOM 1033 OH TYR B 195 92.956 38.656 2.450 1.00 20.00 8 ATOM 1034 C TYR B 195 89.668 34.923 6.160 1.00 20.00 6 ATOM 1035 O TYR B 195 89.409 36.117 6.328 1.00 20.00 8 ATOM 1036 N LEU B 196 88.885 34.103 5.472 1.00 20.00 7 ATOM 1037 CA LEU B 196 87.664 34.576 4.845 1.00 20.00 6 ATOM 1038 CB LEU B 196 86.972 33.426 4.107 1.00 20.00 6 ATOM 1039 CG LEU B 196 85.933 33.824 3.060 1.00 20.00 6 ATOM 1040 CD1 LEU B 196 86.602 34.659 1.966 1.00 20.00 6 ATOM 1041 CD2 LEU B 196 85.305 32.568 2.463 1.00 20.00 6 ATOM 1042 C LEU B 196 86.731 35.161 5.888 1.00 20.00 6 ATOM 1043 O LEU B 196 86.299 36.308 5.774 1.00 20.00 8 ATOM 1044 N HIS B 197 86.431 34.378 6.917 1.00 20.00 7 ATOM 1045 CA HIS B 197 85.533 34.840 7.967 1.00 20.00 6 ATOM 1046 CB HIS B 197 85.241 33.697 8.942 1.00 20.00 6 ATOM 1047 CG HIS B 197 84.377 32.622 8.356 1.00 20.00 6 ATOM 1048 CD2 HIS B 197 83.734 32.550 7.163 1.00 20.00 6 ATOM 1049 ND1 HIS B 197 84.083 31.452 9.022 1.00 20.00 7 ATOM 1050 CE1 HIS B 197 83.296 30.704 8.264 1.00 20.00 6 ATOM 1051 NE2 HIS B 197 83.071 31.346 7.132 1.00 20.00 7 ATOM 1052 C HIS B 197 86.080 36.060 8.697 1.00 20.00 6 ATOM 1053 O HIS B 197 85.314 36.919 9.146 1.00 20.00 8 ATOM 1054 N GLY B 198 87.404 36.143 8.804 1.00 20.00 7 ATOM 1055 CA GLY B 198 88.009 37.285 9.464 1.00 20.00 6 ATOM 1056 C GLY B 198 87.687 38.580 8.737 1.00 20.00 6 ATOM 1057 O GLY B 198 87.784 39.661 9.311 1.00 20.00 8 ATOM 1058 N LYS B 199 87.308 38.475 7.466 1.00 20.00 7 ATOM 1059 CA LYS B 199 86.959 39.652 6.674 1.00 20.00 6 ATOM 1060 CB LYS B 199 87.577 39.573 5.279 1.00 20.00 6 ATOM 1061 CG LYS B 199 89.082 39.736 5.258 1.00 20.00 6 ATOM 1062 CD LYS B 199 89.574 39.919 3.833 1.00 20.00 6 ATOM 1063 CE LYS B 199 91.054 40.243 3.807 1.00 20.00 6 ATOM 1064 NZ LYS B 199 91.398 41.382 4.706 1.00 20.00 7 ATOM 1065 C LYS B 199 85.451 39.804 6.539 1.00 20.00 6 ATOM 1066 O LYS B 199 84.972 40.556 5.693 1.00 20.00 8 ATOM 1067 N GLY B 200 84.707 39.079 7.368 1.00 20.00 7 ATOM 1068 CA GLY B 200 83.258 39.158 7.328 1.00 20.00 6 ATOM 1069 C GLY B 200 82.646 38.660 6.032 1.00 20.00 6 ATOM 1070 O GLY B 200 81.644 39.198 5.564 1.00 20.00 8 ATOM 1071 N ILE B 201 83.243 37.630 5.445 1.00 20.00 7 ATOM 1072 CA ILE B 201 82.726 37.075 4.205 1.00 20.00 6 ATOM 1073 CB ILE B 201 83.775 37.140 3.080 1.00 20.00 6 ATOM 1074 CG2 ILE B 201 83.257 36.413 1.841 1.00 20.00 6 ATOM 1075 CG1 ILE B 201 84.109 38.599 2.761 1.00 20.00 6 ATOM 1076 CD1 ILE B 201 85.330 38.758 1.870 1.00 20.00 6 ATOM 1077 C ILE B 201 82.329 35.623 4.395 1.00 20.00 6 ATOM 1078 O ILE B 201 83.094 34.826 4.942 1.00 20.00 8 ATOM 1079 N ILE B 202 81.125 35.291 3.940 1.00 20.00 7 ATOM 1080 CA ILE B 202 80.592 33.936 4.016 1.00 20.00 6 ATOM 1081 CB ILE B 202 79.119 33.953 4.481 1.00 20.00 6 ATOM 1082 CG2 ILE B 202 78.583 32.522 4.595 1.00 20.00 6 ATOM 1083 CG1 ILE B 202 79.008 34.675 5.825 1.00 20.00 6 ATOM 1084 CD1 ILE B 202 77.576 34.865 6.294 1.00 20.00 6 ATOM 1085 C ILE B 202 80.644 33.393 2.589 1.00 20.00 6 ATOM 1086 O ILE B 202 80.182 34.056 1.663 1.00 20.00 8 ATOM 1087 N HIS B 203 81.204 32.204 2.395 1.00 20.00 7 ATOM 1088 CA HIS B 203 81.279 31.652 1.044 1.00 20.00 6 ATOM 1089 CB HIS B 203 82.258 30.480 0.999 1.00 20.00 6 ATOM 1090 CG HIS B 203 82.478 29.942 −0.380 1.00 20.00 6 ATOM 1091 CD2 HIS B 203 81.646 29.282 −1.220 1.00 20.00 6 ATOM 1092 ND1 HIS B 203 83.659 30.116 −1.069 1.00 20.00 7 ATOM 1093 CE1 HIS B 203 83.545 29.588 −2.275 1.00 20.00 6 ATOM 1094 NE2 HIS B 203 82.333 29.076 −2.392 1.00 20.00 7 ATOM 1095 C HIS B 203 79.896 31.211 0.530 1.00 20.00 6 ATOM 1096 O HIS B 203 79.508 31.546 −0.593 1.00 20.00 8 ATOM 1097 N ARG B 204 79.168 30.458 1.357 1.00 20.00 7 ATOM 1098 CA ARG B 204 77.819 29.969 1.039 1.00 20.00 6 ATOM 1099 CB ARG B 204 76.916 31.117 0.583 1.00 20.00 6 ATOM 1100 CG ARG B 204 76.601 32.120 1.675 1.00 20.00 6 ATOM 1101 CD ARG B 204 75.316 32.878 1.377 1.00 20.00 6 ATOM 1102 NE ARG B 204 75.376 33.616 0.119 1.00 20.00 7 ATOM 1103 CZ ARG B 204 74.423 34.443 −0.303 1.00 20.00 6 ATOM 1104 NH1 ARG B 204 73.336 34.636 0.436 1.00 20.00 7 ATOM 1105 NH2 ARG B 204 74.555 35.084 −1.457 1.00 20.00 7 ATOM 1106 C ARG B 204 77.700 28.829 0.030 1.00 20.00 6 ATOM 1107 O ARG B 204 76.611 28.300 −0.177 1.00 20.00 8 ATOM 1108 N ASP B 205 78.792 28.456 −0.620 1.00 20.00 7 ATOM 1109 CA ASP B 205 78.718 27.342 −1.550 1.00 20.00 6 ATOM 1110 CB ASP B 205 78.380 27.829 −2.961 1.00 20.00 6 ATOM 1111 CG ASP B 205 77.941 26.694 −3.867 1.00 20.00 6 ATOM 1112 OD1 ASP B 205 77.544 25.638 −3.330 1.00 20.00 8 ATOM 1113 OD2 ASP B 205 77.982 26.853 −5.104 1.00 20.00 8 ATOM 1114 C ASP B 205 80.019 26.560 −1.547 1.00 20.00 6 ATOM 1115 O ASP B 205 80.508 26.122 −2.588 1.00 20.00 8 ATOM 1116 N LEU B 206 80.573 26.375 −0.354 1.00 20.00 7 ATOM 1117 CA LEU B 206 81.819 25.652 −0.208 1.00 20.00 6 ATOM 1118 CB LEU B 206 82.361 25.826 1.212 1.00 20.00 6 ATOM 1119 CG LEU B 206 83.764 25.271 1.471 1.00 20.00 6 ATOM 1120 CD1 LEU B 206 84.765 25.969 0.561 1.00 20.00 6 ATOM 1121 CD2 LEU B 206 84.135 25.477 2.933 1.00 20.00 6 ATOM 1122 C LEU B 206 81.609 24.174 −0.514 1.00 20.00 6 ATOM 1123 O LEU B 206 80.691 23.549 0.011 1.00 20.00 8 ATOM 1124 N LYS B 207 82.461 23.628 −1.375 1.00 20.00 7 ATOM 1125 CA LYS B 207 82.379 22.223 −1.765 1.00 20.00 6 ATOM 1126 CB LYS B 207 81.160 22.000 −2.679 1.00 20.00 6 ATOM 1127 CG LYS B 207 81.130 22.913 −3.893 1.00 20.00 6 ATOM 1128 CD LYS B 207 79.876 22.720 −4.736 1.00 20.00 6 ATOM 1129 CE LYS B 207 79.788 23.797 −5.813 1.00 20.00 6 ATOM 1130 NZ LYS B 207 78.695 23.557 −6.791 1.00 20.00 7 ATOM 1131 C LYS B 207 83.657 21.808 −2.487 1.00 20.00 6 ATOM 1132 O LYS B 207 84.416 22.656 −2.960 1.00 20.00 8 ATOM 1133 N PRO B 208 83.916 20.494 −2.582 1.00 20.00 7 ATOM 1134 CD PRO B 208 83.153 19.378 −1.993 1.00 20.00 6 ATOM 1135 CA PRO B 208 85.122 20.005 −3.259 1.00 20.00 6 ATOM 1136 CB PRO B 208 84.922 18.494 −3.267 1.00 20.00 6 ATOM 1137 CG PRO B 208 84.174 18.256 −1.984 1.00 20.00 6 ATOM 1138 C PRO B 208 85.303 20.574 −4.666 1.00 20.00 6 ATOM 1139 O PRO B 208 86.431 20.752 −5.124 1.00 20.00 8 ATOM 1140 N GLU B 209 84.197 20.859 −5.347 1.00 20.00 7 ATOM 1141 CA GLU B 209 84.243 21.410 −6.705 1.00 20.00 6 ATOM 1142 CB GLU B 209 82.836 21.424 −7.317 1.00 20.00 6 ATOM 1143 CG GLU B 209 82.755 22.081 −8.690 1.00 20.00 6 ATOM 1144 CD GLU B 209 81.323 22.296 −9.159 1.00 20.00 6 ATOM 1145 OE1 GLU B 209 80.587 21.299 −9.322 1.00 20.00 8 ATOM 1146 OE2 GLU B 209 80.933 23.465 −9.364 1.00 20.00 8 ATOM 1147 C GLU B 209 84.810 22.836 −6.716 1.00 20.00 6 ATOM 1148 O GLU B 209 85.409 23.269 −7.705 1.00 20.00 8 ATOM 1149 N ASN B 210 84.604 23.549 −5.612 1.00 20.00 7 ATOM 1150 CA ASN B 210 85.051 24.932 −5.439 1.00 20.00 6 ATOM 1151 CB ASN B 210 84.033 25.695 −4.588 1.00 20.00 6 ATOM 1152 CG ASN B 210 82.851 26.170 −5.396 1.00 20.00 6 ATOM 1153 OD1 ASN B 210 81.807 26.520 −4.846 1.00 20.00 8 ATOM 1154 ND2 ASN B 210 83.010 26.194 −6.717 1.00 20.00 7 ATOM 1155 C ASN B 210 86.427 25.070 −4.797 1.00 20.00 6 ATOM 1156 O ASN B 210 86.937 26.181 −4.641 1.00 20.00 8 ATOM 1157 N ILE B 211 87.016 23.948 −4.406 1.00 20.00 7 ATOM 1158 CA ILE B 211 88.331 23.958 −3.790 1.00 20.00 6 ATOM 1159 CB ILE B 211 88.336 23.090 −2.521 1.00 20.00 6 ATOM 1160 CG2 ILE B 211 89.732 23.025 −1.925 1.00 20.00 6 ATOM 1161 CG1 ILE B 211 87.350 23.682 −1.510 1.00 20.00 6 ATOM 1162 CD1 ILE B 211 87.121 22.832 −0.285 1.00 20.00 6 ATOM 1163 C ILE B 211 89.307 23.414 −4.816 1.00 20.00 6 ATOM 1164 O ILE B 211 89.475 22.199 −4.949 1.00 20.00 8 ATOM 1165 N LEU B 212 89.938 24.319 −5.558 1.00 20.00 7 ATOM 1166 CA LEU B 212 90.875 23.918 −6.601 1.00 20.00 6 ATOM 1167 CB LEU B 212 90.966 25.012 −7.673 1.00 20.00 6 ATOM 1168 CG LEU B 212 89.630 25.510 −8.235 1.00 20.00 6 ATOM 1169 CD1 LEU B 212 89.896 26.462 −9.390 1.00 20.00 6 ATOM 1170 CD2 LEU B 212 88.781 24.331 −8.709 1.00 20.00 6 ATOM 1171 C LEU B 212 92.254 23.628 −6.038 1.00 20.00 6 ATOM 1172 O LEU B 212 92.537 23.923 −4.873 1.00 20.00 8 ATOM 1173 N LEU B 213 93.114 23.053 −6.875 1.00 20.00 7 ATOM 1174 CA LEU B 213 94.472 22.714 −6.472 1.00 20.00 6 ATOM 1175 CB LEU B 213 94.609 21.192 −6.388 1.00 20.00 6 ATOM 1176 CG LEU B 213 93.775 20.526 −5.292 1.00 20.00 6 ATOM 1177 CD1 LEU B 213 93.737 19.035 −5.508 1.00 20.00 6 ATOM 1178 CD2 LEU B 213 94.374 20.852 −3.935 1.00 20.00 6 ATOM 1179 C LEU B 213 95.503 23.277 −7.449 1.00 20.00 6 ATOM 1180 O LEU B 213 95.422 23.033 −8.657 1.00 20.00 8 ATOM 1181 N ASN B 214 96.470 24.036 −6.940 1.00 20.00 7 ATOM 1182 CA ASN B 214 97.488 24.585 −7.826 1.00 20.00 6 ATOM 1183 CB ASN B 214 98.198 25.792 −7.201 1.00 20.00 6 ATOM 1184 CG ASN B 214 98.938 25.448 −5.927 1.00 20.00 6 ATOM 1185 OD1 ASN B 214 99.267 24.288 −5.669 1.00 20.00 8 ATOM 1186 ND2 ASN B 214 99.224 26.469 −5.123 1.00 20.00 7 ATOM 1187 C ASN B 214 98.508 23.515 −8.182 1.00 20.00 6 ATOM 1188 O ASN B 214 98.420 22.372 −7.725 1.00 20.00 8 ATOM 1189 N GLU B 215 99.482 23.894 −8.996 1.00 20.00 7 ATOM 1190 CA GLU B 215 100.514 22.965 −9.430 1.00 20.00 6 ATOM 1191 CB GLU B 215 101.491 23.687 −10.362 1.00 20.00 6 ATOM 1192 CG GLU B 215 102.544 22.788 −10.979 1.00 20.00 6 ATOM 1193 CD GLU B 215 103.323 23.482 −12.080 1.00 20.00 6 ATOM 1194 OE1 GLU B 215 103.909 24.554 −11.810 1.00 20.00 8 ATOM 1195 OE2 GLU B 215 103.344 22.957 −13.215 1.00 20.00 8 ATOM 1196 C GLU B 215 101.275 22.307 −8.274 1.00 20.00 6 ATOM 1197 O GLU B 215 101.801 21.205 −8.428 1.00 20.00 8 ATOM 1198 N ASP B 216 101.335 22.976 −7.123 1.00 20.00 7 ATOM 1199 CA ASP B 216 102.036 22.430 −5.958 1.00 20.00 6 ATOM 1200 CB ASP B 216 102.727 23.549 −5.179 1.00 20.00 6 ATOM 1201 CG ASP B 216 103.952 24.086 −5.896 1.00 20.00 6 ATOM 1202 OD1 ASP B 216 104.766 23.267 −6.376 1.00 20.00 8 ATOM 1203 OD2 ASP B 216 104.110 25.323 −5.973 1.00 20.00 8 ATOM 1204 C ASP B 216 101.121 21.651 −5.013 1.00 20.00 6 ATOM 1205 O ASP B 216 101.532 21.241 −3.925 1.00 20.00 8 ATOM 1206 N MET B 217 99.877 21.463 −5.434 1.00 20.00 7 ATOM 1207 CA MET B 217 98.890 20.730 −4.657 1.00 20.00 6 ATOM 1208 CB MET B 217 99.402 19.319 −4.358 1.00 20.00 6 ATOM 1209 CG MET B 217 99.456 18.432 −5.601 1.00 20.00 6 ATOM 1210 SD MET B 217 97.857 18.342 −6.445 1.00 20.00 16 ATOM 1211 CE MET B 217 97.073 16.984 −5.543 1.00 20.00 6 ATOM 1212 C MET B 217 98.397 21.403 −3.373 1.00 20.00 6 ATOM 1213 O MET B 217 97.972 20.730 −2.435 1.00 20.00 8 ATOM 1214 N HIS B 218 98.469 22.730 −3.331 1.00 20.00 7 ATOM 1215 CA HIS B 218 97.949 23.487 −2.197 1.00 20.00 6 ATOM 1216 CB HIS B 218 98.831 24.700 −1.898 1.00 20.00 6 ATOM 1217 CG HIS B 218 100.100 24.357 −1.177 1.00 20.00 6 ATOM 1218 CD2 HIS B 218 101.390 24.362 −1.588 1.00 20.00 6 ATOM 1219 ND1 HIS B 218 100.117 23.935 0.136 1.00 20.00 7 ATOM 1220 CE1 HIS B 218 101.364 23.698 0.504 1.00 20.00 6 ATOM 1221 NE2 HIS B 218 102.156 23.947 −0.524 1.00 20.00 7 ATOM 1222 C HIS B 218 96.583 23.939 −2.703 1.00 20.00 6 ATOM 1223 O HIS B 218 96.400 24.090 −3.910 1.00 20.00 8 ATOM 1224 N ILE B 219 95.628 24.160 −1.808 1.00 20.00 7 ATOM 1225 CA ILE B 219 94.301 24.562 −2.257 1.00 20.00 6 ATOM 1226 CB ILE B 219 93.232 24.359 −1.159 1.00 20.00 6 ATOM 1227 CG2 ILE B 219 93.266 22.918 −0.654 1.00 20.00 6 ATOM 1228 CG1 ILE B 219 93.460 25.353 −0.011 1.00 20.00 6 ATOM 1229 CD1 ILE B 219 92.351 25.342 1.036 1.00 20.00 6 ATOM 1230 C ILE B 219 94.207 26.010 −2.714 1.00 20.00 6 ATOM 1231 O ILE B 219 95.044 26.850 −2.375 1.00 20.00 8 ATOM 1232 N GLN B 220 93.168 26.274 −3.497 1.00 20.00 7 ATOM 1233 CA GLN B 220 92.859 27.600 −3.999 1.00 20.00 6 ATOM 1234 CB GLN B 220 93.537 27.867 −5.350 1.00 20.00 6 ATOM 1235 CG GLN B 220 95.011 28.246 −5.216 1.00 20.00 6 ATOM 1236 CD GLN B 220 95.599 28.799 −6.503 1.00 20.00 6 ATOM 1237 OE1 GLN B 220 95.725 28.086 −7.502 1.00 20.00 8 ATOM 1238 NE2 GLN B 220 95.957 30.079 −6.486 1.00 20.00 7 ATOM 1239 C GLN B 220 91.350 27.626 −4.140 1.00 20.00 6 ATOM 1240 O GLN B 220 90.792 27.133 −5.124 1.00 20.00 8 ATOM 1241 N ILE B 221 90.689 28.178 −3.129 1.00 20.00 7 ATOM 1242 CA ILE B 221 89.240 28.260 −3.122 1.00 20.00 6 ATOM 1243 CB ILE B 221 88.731 28.550 −1.700 1.00 20.00 6 ATOM 1244 CG2 ILE B 221 87.209 28.707 −1.708 1.00 20.00 6 ATOM 1245 CG1 ILE B 221 89.164 27.406 −0.773 1.00 20.00 6 ATOM 1246 CD1 ILE B 221 88.743 27.559 0.668 1.00 20.00 6 ATOM 1247 C ILE B 221 88.760 29.339 −4.092 1.00 20.00 6 ATOM 1248 O ILE B 221 89.411 30.374 −4.262 1.00 20.00 8 ATOM 1249 N THR B 222 87.633 29.082 −4.748 1.00 20.00 7 ATOM 1250 CA THR B 222 87.084 30.039 −5.701 1.00 20.00 6 ATOM 1251 CB THR B 222 87.565 29.728 −7.125 1.00 20.00 6 ATOM 1252 OG1 THR B 222 87.179 30.795 −8.000 1.00 20.00 8 ATOM 1253 CG2 THR B 222 86.962 28.410 −7.618 1.00 20.00 6 ATOM 1254 C THR B 222 85.554 30.028 −5.683 1.00 20.00 6 ATOM 1255 O THR B 222 84.950 29.417 −4.791 1.00 20.00 8 ATOM 1256 N ASP B 223 84.949 30.712 −6.659 1.00 20.00 7 ATOM 1257 CA ASP B 223 83.492 30.806 −6.806 1.00 20.00 6 ATOM 1258 CB ASP B 223 82.872 29.399 −6.767 1.00 20.00 6 ATOM 1259 CG ASP B 223 81.414 29.384 −7.205 1.00 20.00 6 ATOM 1260 OD1 ASP B 223 80.990 30.335 −7.900 1.00 20.00 8 ATOM 1261 OD2 ASP B 223 80.701 28.414 −6.866 1.00 20.00 8 ATOM 1262 C ASP B 223 82.878 31.694 −5.725 1.00 20.00 6 ATOM 1263 O ASP B 223 82.191 31.208 −4.820 1.00 20.00 8 ATOM 1264 N PHE B 224 83.105 33.001 −5.848 1.00 20.00 7 ATOM 1265 CA PHE B 224 82.632 33.970 −4.866 1.00 20.00 6 ATOM 1266 CB PHE B 224 83.800 34.869 −4.451 1.00 20.00 6 ATOM 1267 CG PHE B 224 84.826 34.165 −3.612 1.00 20.00 6 ATOM 1268 CD1 PHE B 224 84.590 33.931 −2.261 1.00 20.00 6 ATOM 1269 CD2 PHE B 224 86.001 33.687 −4.182 1.00 20.00 6 ATOM 1270 CE1 PHE B 224 85.509 33.227 −1.486 1.00 20.00 6 ATOM 1271 CE2 PHE B 224 86.927 32.981 −3.418 1.00 20.00 6 ATOM 1272 CZ PHE B 224 86.679 32.750 −2.068 1.00 20.00 6 ATOM 1273 C PHE B 224 81.443 34.839 −5.256 1.00 20.00 6 ATOM 1274 O PHE B 224 81.001 35.678 −4.468 1.00 20.00 8 ATOM 1275 N GLY B 225 80.928 34.647 −6.463 1.00 20.00 7 ATOM 1276 CA GLY B 225 79.793 35.438 −6.894 1.00 20.00 6 ATOM 1277 C GLY B 225 78.612 35.265 −5.955 1.00 20.00 6 ATOM 1278 O GLY B 225 77.824 36.192 −5.753 1.00 20.00 8 ATOM 1279 N THR B 226 78.486 34.080 −5.367 1.00 20.00 7 ATOM 1280 CA THR B 226 77.379 33.819 −4.459 1.00 20.00 6 ATOM 1281 CB THR B 226 76.779 32.425 −4.715 1.00 20.00 6 ATOM 1282 OG1 THR B 226 77.826 31.450 −4.762 1.00 20.00 8 ATOM 1283 CG2 THR B 226 76.021 32.417 −6.041 1.00 20.00 6 ATOM 1284 C THR B 226 77.738 33.957 −2.981 1.00 20.00 6 ATOM 1285 O THR B 226 77.001 33.500 −2.107 1.00 20.00 8 ATOM 1286 N ALA B 227 78.867 34.598 −2.702 1.00 20.00 7 ATOM 1287 CA ALA B 227 79.282 34.800 −1.325 1.00 20.00 6 ATOM 1288 CB ALA B 227 80.738 35.242 −1.268 1.00 20.00 6 ATOM 1289 C ALA B 227 78.384 35.875 −0.726 1.00 20.00 6 ATOM 1290 O ALA B 227 77.623 36.529 −1.440 1.00 20.00 8 ATOM 1291 N LYS B 228 78.467 36.046 0.586 1.00 20.00 7 ATOM 1292 CA LYS B 228 77.670 37.051 1.274 1.00 20.00 6 ATOM 1293 CB LYS B 228 76.637 36.384 2.179 1.00 20.00 6 ATOM 1294 CG LYS B 228 75.705 37.357 2.890 1.00 20.00 6 ATOM 1295 CD LYS B 228 74.795 38.072 1.893 1.00 20.00 6 ATOM 1296 CE LYS B 228 73.849 39.049 2.587 1.00 20.00 6 ATOM 1297 NZ LYS B 228 73.000 39.781 1.605 1.00 20.00 7 ATOM 1298 C LYS B 228 78.616 37.896 2.110 1.00 20.00 6 ATOM 1299 O LYS B 228 79.355 37.366 2.940 1.00 20.00 8 ATOM 1300 N VAL B 229 78.603 39.206 1.881 1.00 20.00 7 ATOM 1301 CA VAL B 229 79.463 40.114 2.626 1.00 20.00 6 ATOM 1302 CB VAL B 229 79.976 41.256 1.734 1.00 20.00 6 ATOM 1303 CG1 VAL B 229 80.853 42.191 2.540 1.00 20.00 6 ATOM 1304 CG2 VAL B 229 80.746 40.686 0.561 1.00 20.00 6 ATOM 1305 C VAL B 229 78.687 40.710 3.793 1.00 20.00 6 ATOM 1306 O VAL B 229 77.798 41.537 3.599 1.00 20.00 8 ATOM 1307 N LEU B 230 79.034 40.284 5.003 1.00 20.00 7 ATOM 1308 CA LEU B 230 78.370 40.752 6.213 1.00 20.00 6 ATOM 1309 CB LEU B 230 78.740 39.856 7.395 1.00 20.00 6 ATOM 1310 CG LEU B 230 78.276 38.403 7.332 1.00 20.00 6 ATOM 1311 CD1 LEU B 230 78.853 37.634 8.508 1.00 20.00 6 ATOM 1312 CD2 LEU B 230 76.760 38.350 7.339 1.00 20.00 6 ATOM 1313 C LEU B 230 78.705 42.193 6.565 1.00 20.00 6 ATOM 1314 O LEU B 230 79.768 42.701 6.214 1.00 20.00 8 ATOM 1315 N SER B 231 77.781 42.839 7.270 1.00 20.00 7 ATOM 1316 CA SER B 231 77.957 44.219 7.708 1.00 20.00 6 ATOM 1317 CB SER B 231 77.082 45.161 6.875 1.00 20.00 6 ATOM 1318 OG SER B 231 75.714 44.795 6.948 1.00 20.00 8 ATOM 1319 C SER B 231 77.623 44.373 9.196 1.00 20.00 6 ATOM 1320 O SER B 231 78.322 45.086 9.919 1.00 20.00 8 ATOM 1321 N PRO B 232 76.553 43.705 9.674 1.00 20.00 7 ATOM 1322 CD PRO B 232 75.571 42.876 8.948 1.00 20.00 6 ATOM 1323 CA PRO B 232 76.182 43.811 11.091 1.00 20.00 6 ATOM 1324 CB PRO B 232 75.005 42.844 11.211 1.00 20.00 6 ATOM 1325 CG PRO B 232 74.367 42.933 9.862 1.00 20.00 6 ATOM 1326 C PRO B 232 77.332 43.438 12.024 1.00 20.00 6 ATOM 1327 O PRO B 232 78.199 42.640 11.666 1.00 20.00 8 ATOM 1328 N ALA B 237 74.215 38.132 11.762 1.00 20.00 7 ATOM 1329 CA ALA B 237 74.666 37.653 10.460 1.00 20.00 6 ATOM 1330 CB ALA B 237 75.541 36.417 10.637 1.00 20.00 6 ATOM 1331 C ALA B 237 73.479 37.324 9.558 1.00 20.00 6 ATOM 1332 O ALA B 237 73.143 36.158 9.374 1.00 20.00 8 ATOM 1333 N ALA B 238 72.841 38.347 8.996 1.00 20.00 7 ATOM 1334 CA ALA B 238 71.693 38.130 8.117 1.00 20.00 6 ATOM 1335 CB ALA B 238 70.973 39.450 7.853 1.00 20.00 6 ATOM 1336 C ALA B 238 72.123 37.497 6.798 1.00 20.00 6 ATOM 1337 O ALA B 238 73.315 37.404 6.500 1.00 20.00 8 ATOM 1338 N ALA B 239 71.146 37.057 6.012 1.00 20.00 7 ATOM 1339 CA ALA B 239 71.439 36.431 4.728 1.00 20.00 6 ATOM 1340 CB ALA B 239 72.152 35.123 4.952 1.00 20.00 6 ATOM 1341 C ALA B 239 70.173 36.194 3.918 1.00 20.00 6 ATOM 1342 O ALA B 239 69.329 37.079 3.825 1.00 20.00 8 ATOM 1343 N ASN B 240 70.068 34.996 3.339 1.00 20.00 7 ATOM 1344 CA ASN B 240 68.939 34.559 2.514 1.00 20.00 6 ATOM 1345 CB ASN B 240 67.614 35.160 2.999 1.00 20.00 6 ATOM 1346 CG ASN B 240 67.258 36.466 2.299 1.00 20.00 6 ATOM 1347 OD1 ASN B 240 67.119 36.519 1.068 1.00 20.00 8 ATOM 1348 ND2 ASN B 240 67.091 37.536 3.089 1.00 20.00 7 ATOM 1349 C ASN B 240 69.153 34.937 1.053 1.00 20.00 6 ATOM 1350 O ASN B 240 70.007 35.767 0.749 1.00 20.00 8 ATOM 1351 N ALA B 241 68.365 34.329 0.163 1.00 20.00 7 ATOM 1352 CA ALA B 241 68.401 34.570 −1.290 1.00 20.00 6 ATOM 1353 C ALA B 241 68.990 33.416 −2.103 1.00 20.00 6 ATOM 1354 O ALA B 241 68.353 32.919 −3.030 1.00 20.00 8 ATOM 1355 CB ALA B 241 69.168 35.859 −1.629 1.00 20.00 6 ATOM 1356 N PHE B 242 70.205 33.000 −1.762 1.00 20.00 7 ATOM 1357 CA PHE B 242 70.875 31.918 −2.481 1.00 20.00 6 ATOM 1358 CB PHE B 242 72.259 32.379 −2.952 1.00 20.00 6 ATOM 1359 CG PHE B 242 73.102 31.273 −3.521 1.00 20.00 6 ATOM 1360 CD1 PHE B 242 72.843 30.767 −4.790 1.00 20.00 6 ATOM 1361 CD2 PHE B 242 74.136 30.713 −2.773 1.00 20.00 6 ATOM 1362 CE1 PHE B 242 73.599 29.718 −5.310 1.00 20.00 6 ATOM 1363 CE2 PHE B 242 74.896 29.666 −3.281 1.00 20.00 6 ATOM 1364 CZ PHE B 242 74.627 29.166 −4.553 1.00 20.00 6 ATOM 1365 C PHE B 242 71.038 30.652 −1.646 1.00 20.00 6 ATOM 1366 O PHE B 242 71.213 30.716 −0.431 1.00 20.00 8 ATOM 1367 N VAL B 243 70.988 29.505 −2.318 1.00 20.00 7 ATOM 1368 CA VAL B 243 71.157 28.204 −1.675 1.00 20.00 6 ATOM 1369 CB VAL B 243 69.828 27.420 −1.617 1.00 20.00 6 ATOM 1370 CG1 VAL B 243 70.066 26.023 −1.050 1.00 20.00 6 ATOM 1371 CG2 VAL B 243 68.825 28.177 −0.766 1.00 20.00 6 ATOM 1372 C VAL B 243 72.164 27.394 −2.486 1.00 20.00 6 ATOM 1373 O VAL B 243 71.894 27.014 −3.628 1.00 20.00 8 ATOM 1374 N GLY B 244 73.323 27.137 −1.890 1.00 20.00 7 ATOM 1375 CA GLY B 244 74.364 26.385 −2.569 1.00 20.00 6 ATOM 1376 C GLY B 244 74.019 24.944 −2.911 1.00 20.00 6 ATOM 1377 O GLY B 244 72.867 24.524 −2.810 1.00 20.00 8 ATOM 1378 N THR B 245 75.032 24.184 −3.315 1.00 20.00 7 ATOM 1379 CA THR B 245 74.858 22.787 −3.691 1.00 20.00 6 ATOM 1380 CB THR B 245 76.214 22.161 −4.046 1.00 20.00 6 ATOM 1381 OG1 THR B 245 76.794 22.911 −5.120 1.00 20.00 8 ATOM 1382 CG2 THR B 245 76.049 20.710 −4.485 1.00 20.00 6 ATOM 1383 C THR B 245 74.174 22.003 −2.579 1.00 20.00 6 ATOM 1384 O THR B 245 74.643 21.969 −1.441 1.00 20.00 8 ATOM 1385 N ALA B 246 73.061 21.372 −2.937 1.00 20.00 7 ATOM 1386 CA ALA B 246 72.229 20.615 −2.008 1.00 20.00 6 ATOM 1387 CB ALA B 246 71.266 19.723 −2.793 1.00 20.00 6 ATOM 1388 C ALA B 246 72.936 19.789 −0.941 1.00 20.00 6 ATOM 1389 O ALA B 246 72.611 19.894 0.239 1.00 20.00 8 ATOM 1390 N GLN B 247 73.902 18.973 −1.339 1.00 20.00 7 ATOM 1391 CA GLN B 247 74.580 18.121 −0.371 1.00 20.00 6 ATOM 1392 CB GLN B 247 75.535 17.168 −1.096 1.00 20.00 6 ATOM 1393 CG GLN B 247 75.110 16.823 −2.520 1.00 20.00 6 ATOM 1394 CD GLN B 247 75.139 15.336 −2.811 1.00 20.00 6 ATOM 1395 OE1 GLN B 247 75.963 14.602 −2.270 1.00 20.00 8 ATOM 1396 NE2 GLN B 247 74.246 14.887 −3.686 1.00 20.00 7 ATOM 1397 C GLN B 247 75.343 18.873 0.720 1.00 20.00 6 ATOM 1398 O GLN B 247 75.631 18.306 1.773 1.00 20.00 8 ATOM 1399 N TYR B 248 75.648 20.147 0.484 1.00 20.00 7 ATOM 1400 CA TYR B 248 76.405 20.941 1.454 1.00 20.00 6 ATOM 1401 CB TYR B 248 77.642 21.531 0.767 1.00 20.00 6 ATOM 1402 CG TYR B 248 78.447 20.471 0.052 1.00 20.00 6 ATOM 1403 CD1 TYR B 248 79.329 19.648 0.750 1.00 20.00 6 ATOM 1404 CE1 TYR B 248 79.979 18.589 0.115 1.00 20.00 6 ATOM 1405 CD2 TYR B 248 78.243 20.220 −1.306 1.00 20.00 6 ATOM 1406 CE2 TYR B 248 78.884 19.167 −1.951 1.00 20.00 6 ATOM 1407 CZ TYR B 248 79.748 18.352 −1.232 1.00 20.00 6 ATOM 1408 OH TYR B 248 80.348 17.280 −1.852 1.00 20.00 8 ATOM 1409 C TYR B 248 75.596 22.055 2.118 1.00 20.00 6 ATOM 1410 O TYR B 248 76.132 22.824 2.917 1.00 20.00 8 ATOM 1411 N VAL B 249 74.309 22.135 1.798 1.00 20.00 7 ATOM 1412 CA VAL B 249 73.452 23.162 2.376 1.00 20.00 6 ATOM 1413 CB VAL B 249 72.071 23.174 1.695 1.00 20.00 6 ATOM 1414 CG1 VAL B 249 71.117 24.100 2.442 1.00 20.00 6 ATOM 1415 CG2 VAL B 249 72.225 23.632 0.264 1.00 20.00 6 ATOM 1416 C VAL B 249 73.262 22.964 3.875 1.00 20.00 6 ATOM 1417 O VAL B 249 73.027 21.847 4.341 1.00 20.00 8 ATOM 1418 N SER B 250 73.373 24.055 4.628 1.00 20.00 7 ATOM 1419 CA SER B 250 73.206 24.008 6.076 1.00 20.00 6 ATOM 1420 CB SER B 250 73.921 25.198 6.738 1.00 20.00 6 ATOM 1421 OG SER B 250 73.428 26.440 6.257 1.00 20.00 8 ATOM 1422 C SER B 250 71.717 24.049 6.405 1.00 20.00 6 ATOM 1423 O SER B 250 70.920 24.577 5.636 1.00 20.00 8 ATOM 1424 N PRO B 251 71.322 23.479 7.550 1.00 20.00 7 ATOM 1425 CD PRO B 251 72.130 22.770 8.558 1.00 20.00 6 ATOM 1426 CA PRO B 251 69.905 23.484 7.925 1.00 20.00 6 ATOM 1427 CB PRO B 251 69.892 22.714 9.252 1.00 20.00 6 ATOM 1428 CG PRO B 251 71.290 22.936 9.801 1.00 20.00 6 ATOM 1429 C PRO B 251 69.265 24.870 8.032 1.00 20.00 6 ATOM 1430 O PRO B 251 68.093 25.036 7.688 1.00 20.00 8 ATOM 1431 N GLU B 252 70.017 25.867 8.492 1.00 20.00 7 ATOM 1432 CA GLU B 252 69.462 27.216 8.625 1.00 20.00 6 ATOM 1433 CB GLU B 252 70.503 28.193 9.196 1.00 20.00 6 ATOM 1434 CG GLU B 252 71.838 28.180 8.477 1.00 20.00 6 ATOM 1435 CD GLU B 252 72.844 27.257 9.139 1.00 20.00 6 ATOM 1436 OE1 GLU B 252 72.429 26.207 9.675 1.00 20.00 8 ATOM 1437 OE2 GLU B 252 74.053 27.581 9.118 1.00 20.00 8 ATOM 1438 C GLU B 252 68.928 27.744 7.292 1.00 20.00 6 ATOM 1439 O GLU B 252 67.927 28.459 7.261 1.00 20.00 8 ATOM 1440 N LEU B 253 69.584 27.395 6.189 1.00 20.00 7 ATOM 1441 CA LEU B 253 69.117 27.850 4.883 1.00 20.00 6 ATOM 1442 CB LEU B 253 70.140 27.527 3.794 1.00 20.00 6 ATOM 1443 CG LEU B 253 71.127 28.635 3.421 1.00 20.00 6 ATOM 1444 CD1 LEU B 253 72.121 28.851 4.547 1.00 20.00 6 ATOM 1445 CD2 LEU B 253 71.858 28.250 2.140 1.00 20.00 6 ATOM 1446 C LEU B 253 67.774 27.227 4.496 1.00 20.00 6 ATOM 1447 O LEU B 253 66.997 27.826 3.751 1.00 20.00 8 ATOM 1448 N LEU B 254 67.506 26.029 5.002 1.00 20.00 7 ATOM 1449 CA LEU B 254 66.271 25.316 4.689 1.00 20.00 6 ATOM 1450 CB LEU B 254 66.539 23.809 4.689 1.00 20.00 6 ATOM 1451 CG LEU B 254 67.647 23.322 3.746 1.00 20.00 6 ATOM 1452 CD1 LEU B 254 67.983 21.873 4.057 1.00 20.00 6 ATOM 1453 CD2 LEU B 254 67.204 23.475 2.302 1.00 20.00 6 ATOM 1454 C LEU B 254 65.135 25.626 5.662 1.00 20.00 6 ATOM 1455 O LEU B 254 63.959 25.524 5.312 1.00 20.00 8 ATOM 1456 N THR B 255 65.483 26.010 6.883 1.00 20.00 7 ATOM 1457 CA THR B 255 64.472 26.308 7.884 1.00 20.00 6 ATOM 1458 CB THR B 255 64.876 25.747 9.252 1.00 20.00 6 ATOM 1459 OG1 THR B 255 66.154 26.277 9.619 1.00 20.00 8 ATOM 1460 CG2 THR B 255 64.958 24.230 9.202 1.00 20.00 6 ATOM 1461 C THR B 255 64.205 27.795 8.035 1.00 20.00 6 ATOM 1462 O THR B 255 63.072 28.241 7.897 1.00 20.00 8 ATOM 1463 N GLU B 256 65.250 28.560 8.314 1.00 20.00 7 ATOM 1464 CA GLU B 256 65.115 30.001 8.507 1.00 20.00 6 ATOM 1465 CB GLU B 256 66.015 30.444 9.659 1.00 20.00 6 ATOM 1466 CG GLU B 256 65.634 29.818 10.987 1.00 20.00 6 ATOM 1467 CD GLU B 256 66.736 29.922 12.018 1.00 20.00 6 ATOM 1468 OE1 GLU B 256 67.249 31.041 12.232 1.00 20.00 8 ATOM 1469 OE2 GLU B 256 67.086 28.884 12.619 1.00 20.00 8 ATOM 1470 C GLU B 256 65.439 30.815 7.262 1.00 20.00 6 ATOM 1471 O GLU B 256 65.268 32.034 7.252 1.00 20.00 8 ATOM 1472 N LYS B 257 65.906 30.141 6.215 1.00 20.00 7 ATOM 1473 CA LYS B 257 66.260 30.814 4.970 1.00 20.00 6 ATOM 1474 CB LYS B 257 65.015 31.458 4.352 1.00 20.00 6 ATOM 1475 CG LYS B 257 65.184 31.918 2.915 1.00 20.00 6 ATOM 1476 CD LYS B 257 63.885 32.497 2.378 1.00 20.00 6 ATOM 1477 CE LYS B 257 63.994 32.841 0.902 1.00 20.00 6 ATOM 1478 NZ LYS B 257 65.060 33.847 0.640 1.00 20.00 7 ATOM 1479 C LYS B 257 67.309 31.885 5.263 1.00 20.00 6 ATOM 1480 O LYS B 257 67.270 32.977 4.702 1.00 20.00 8 ATOM 1481 N SER B 258 68.243 31.563 6.152 1.00 20.00 7 ATOM 1482 CA SER B 258 69.300 32.494 6.527 1.00 20.00 6 ATOM 1483 CB SER B 258 69.043 33.028 7.937 1.00 20.00 6 ATOM 1484 OG SER B 258 68.893 31.962 8.859 1.00 20.00 8 ATOM 1485 C SER B 258 70.675 31.829 6.467 1.00 20.00 6 ATOM 1486 O SER B 258 70.786 30.602 6.542 1.00 20.00 8 ATOM 1487 N ALA B 259 71.718 32.641 6.329 1.00 20.00 7 ATOM 1488 CA ALA B 259 73.081 32.130 6.252 1.00 20.00 6 ATOM 1489 CB ALA B 259 73.549 32.121 4.809 1.00 20.00 6 ATOM 1490 C ALA B 259 74.031 32.966 7.102 1.00 20.00 6 ATOM 1491 O ALA B 259 73.882 34.185 7.211 1.00 20.00 8 ATOM 1492 N CYS B 260 75.008 32.298 7.704 1.00 20.00 7 ATOM 1493 CA CYS B 260 75.993 32.960 8.550 1.00 20.00 6 ATOM 1494 CB CYS B 260 75.574 32.865 10.017 1.00 20.00 6 ATOM 1495 SG CYS B 260 75.303 31.165 10.594 1.00 20.00 16 ATOM 1496 C GYS B 260 77.328 32.265 8.349 1.00 20.00 6 ATOM 1497 O CYS B 260 77.410 31.280 7.620 1.00 20.00 8 ATOM 1498 N LYS B 261 78.371 32.775 8.993 1.00 20.00 7 ATOM 1499 CA LYS B 261 79.691 32.174 8.869 1.00 20.00 6 ATOM 1500 CB LYS B 261 80.676 32.851 9.821 1.00 20.00 6 ATOM 1501 CG LYS B 261 80.985 34.296 9.472 1.00 20.00 6 ATOM 1502 CD LYS B 261 81.961 34.878 10.475 1.00 20.00 6 ATOM 1503 CE LYS B 261 82.157 36.365 10.259 1.00 20.00 6 ATOM 1504 NZ LYS B 261 83.085 36.922 11.278 1.00 20.00 7 ATOM 1505 C LYS B 261 79.632 30.687 9.187 1.00 20.00 6 ATOM 1506 O LYS B 261 80.258 29.877 8.512 1.00 20.00 8 ATOM 1507 N SER B 262 78.860 30.346 10.214 1.00 20.00 7 ATOM 1508 CA SER B 262 78.716 28.966 10.659 1.00 20.00 6 ATOM 1509 CB SER B 262 77.806 28.913 11.895 1.00 20.00 6 ATOM 1510 OG SER B 262 77.884 27.657 12.546 1.00 20.00 8 ATOM 1511 C SER B 262 78.161 28.070 9.549 1.00 20.00 6 ATOM 1512 O SER B 262 78.350 26.856 9.575 1.00 20.00 8 ATOM 1513 N SER B 263 77.466 28.660 8.581 1.00 20.00 7 ATOM 1514 CA SER B 263 76.938 27.870 7.472 1.00 20.00 6 ATOM 1515 CB SER B 263 76.132 28.750 6.507 1.00 20.00 6 ATOM 1516 OG SER B 263 75.011 29.329 7.156 1.00 20.00 8 ATOM 1517 C SER B 263 78.123 27.244 6.737 1.00 20.00 6 ATOM 1518 O SER B 263 78.038 26.108 6.273 1.00 20.00 8 ATOM 1519 N ASP B 264 79.234 27.977 6.642 1.00 20.00 7 ATOM 1520 CA ASP B 264 80.419 27.448 5.961 1.00 20.00 6 ATOM 1521 CB ASP B 264 81.478 28.538 5.745 1.00 20.00 6 ATOM 1522 CG ASP B 264 81.091 29.539 4.673 1.00 20.00 6 ATOM 1523 OD1 ASP B 264 80.286 29.187 3.786 1.00 20.00 8 ATOM 1524 OD2 ASP B 264 81.617 30.676 4.704 1.00 20.00 8 ATOM 1525 C ASP B 264 81.043 26.312 6.771 1.00 20.00 6 ATOM 1526 O ASP B 264 81.586 25.365 6.201 1.00 20.00 8 ATOM 1527 N LEU B 265 80.971 26.415 8.099 1.00 20.00 7 ATOM 1528 CA LEU B 265 81.532 25.390 8.974 1.00 20.00 6 ATOM 1529 CB LEU B 265 81.491 25.848 10.438 1.00 20.00 6 ATOM 1530 CG LEU B 265 82.419 27.035 10.746 1.00 20.00 6 ATOM 1531 CD1 LEU B 265 82.204 27.532 12.177 1.00 20.00 6 ATOM 1532 CD2 LEU B 265 83.864 26.608 10.541 1.00 20.00 6 ATOM 1533 C LEU B 265 80.750 24.094 8.800 1.00 20.00 6 ATOM 1534 O LEU B 265 81.306 23.004 8.910 1.00 20.00 8 ATOM 1535 N TRP B 266 79.454 24.208 8.530 1.00 20.00 7 ATOM 1536 CA TRP B 266 78.646 23.017 8.309 1.00 20.00 6 ATOM 1537 CB TRP B 266 77.167 23.384 8.148 1.00 20.00 6 ATOM 1538 CG TRP B 266 76.310 22.245 7.646 1.00 20.00 6 ATOM 1539 CD2 TRP B 266 75.455 21.399 8.426 1.00 20.00 6 ATOM 1540 CE2 TRP B 266 74.881 20.455 7.542 1.00 20.00 6 ATOM 1541 CE3 TRP B 266 75.117 21.345 9.785 1.00 20.00 6 ATOM 1542 CD1 TRP B 266 76.220 21.792 6.356 1.00 20.00 6 ATOM 1543 NE1 TRP B 266 75.365 20.719 6.288 1.00 20.00 7 ATOM 1544 CZ2 TRP B 266 73.988 19.466 7.975 1.00 20.00 6 ATOM 1545 CZ3 TRP B 266 74.227 20.359 10.216 1.00 20.00 6 ATOM 1546 CH2 TRP B 266 73.674 19.434 9.310 1.00 20.00 6 ATOM 1547 C TRP B 266 79.169 22.356 7.038 1.00 20.00 6 ATOM 1548 O TRP B 266 79.356 21.142 6.988 1.00 20.00 8 ATOM 1549 N ALA B 267 79.411 23.164 6.011 1.00 20.00 7 ATOM 1550 CA ALA B 267 79.930 22.646 4.751 1.00 20.00 6 ATOM 1551 CB ALA B 267 80.089 23.772 3.746 1.00 20.00 6 ATOM 1552 C ALA B 267 81.277 21.976 5.016 1.00 20.00 6 ATOM 1553 O ALA B 267 81.570 20.914 4.471 1.00 20.00 8 ATOM 1554 N LEU B 268 82.091 22.596 5.864 1.00 20.00 7 ATOM 1555 CA LEU B 268 83.393 22.030 6.209 1.00 20.00 6 ATOM 1556 CB LEU B 268 84.092 22.898 7.264 1.00 20.00 6 ATOM 1557 CG LEU B 268 85.379 22.332 7.879 1.00 20.00 6 ATOM 1558 CD1 LEU B 268 86.442 22.192 6.803 1.00 20.00 6 ATOM 1559 CD2 LEU B 268 85.872 23.263 9.006 1.00 20.00 6 ATOM 1560 C LEU B 268 83.193 20.617 6.753 1.00 20.00 6 ATOM 1561 O LEU B 268 83.903 19.684 6.372 1.00 20.00 8 ATOM 1562 N GLY B 269 82.220 20.463 7.645 1.00 20.00 7 ATOM 1563 CA GLY B 269 81.947 19.156 8.217 1.00 20.00 6 ATOM 1564 C GLY B 269 81.597 18.125 7.156 1.00 20.00 6 ATOM 1565 O GLY B 269 82.025 16.971 7.239 1.00 20.00 8 ATOM 1566 N CYS B 270 80.819 18.530 6.155 1.00 20.00 7 ATOM 1567 CA CYS B 270 80.445 17.613 5.083 1.00 20.00 6 ATOM 1568 CB CYS B 270 79.413 18.255 4.148 1.00 20.00 6 ATOM 1569 SG CYS B 270 77.824 18.654 4.905 1.00 20.00 16 ATOM 1570 C GYS B 270 81.682 17.241 4.265 1.00 20.00 6 ATOM 1571 O CYS B 270 81.852 16.090 3.866 1.00 20.00 8 ATOM 1572 N ILE B 271 82.541 18.226 4.012 1.00 20.00 7 ATOM 1573 CA ILE B 271 83.751 18.000 3.229 1.00 20.00 6 ATOM 1574 CB ILE B 271 84.436 19.339 2.903 1.00 20.00 6 ATOM 1575 CG2 ILE B 271 85.784 19.098 2.227 1.00 20.00 6 ATOM 1576 CG1 ILE B 271 83.508 20.171 2.007 1.00 20.00 6 ATOM 1577 CD1 ILE B 271 83.962 21.607 1.815 1.00 20.00 6 ATOM 1578 C ILE B 271 84.729 17.063 3.934 1.00 20.00 6 ATOM 1579 O ILE B 271 85.300 16.174 3.304 1.00 20.00 8 ATOM 1580 N ILE B 272 84.927 17.258 5.236 1.00 20.00 7 ATOM 1581 CA ILE B 272 85.820 16.382 5.987 1.00 20.00 6 ATOM 1582 CB ILE B 272 85.902 16.790 7.471 1.00 20.00 6 ATOM 1583 CG2 ILE B 272 86.623 15.703 8.277 1.00 20.00 6 ATOM 1584 CG1 ILE B 272 86.646 18.120 7.606 1.00 20.00 6 ATOM 1585 CD1 ILE B 272 86.553 18.723 9.011 1.00 20.00 6 ATOM 1586 C ILE B 272 85.274 14.957 5.901 1.00 20.00 6 ATOM 1587 O ILE B 272 86.021 14.003 5.679 1.00 20.00 8 ATOM 1588 N TYR B 273 83.964 14.822 6.072 1.00 20.00 7 ATOM 1589 CA TYR B 273 83.324 13.518 6.006 1.00 20.00 6 ATOM 1590 CB TYR B 273 81.825 13.651 6.287 1.00 20.00 6 ATOM 1591 CG TYR B 273 81.064 12.340 6.250 1.00 20.00 6 ATOM 1592 CD1 TYR B 273 80.806 11.690 5.041 1.00 20.00 6 ATOM 1593 CE1 TYR B 273 80.107 10.486 5.005 1.00 20.00 6 ATOM 1594 CD2 TYR B 273 80.601 11.750 7.427 1.00 20.00 6 ATOM 1595 CE2 TYR B 273 79.904 10.548 7.405 1.00 20.00 6 ATOM 1596 CZ TYR B 273 79.659 9.922 6.192 1.00 20.00 6 ATOM 1597 OH TYR B 273 78.971 8.736 6.174 1.00 20.00 8 ATOM 1598 C TYR B 273 83.550 12.897 4.632 1.00 20.00 6 ATOM 1599 O TYR B 273 83.865 11.713 4.526 1.00 20.00 8 ATOM 1600 N GLN B 274 83.402 13.705 3.586 1.00 20.00 7 ATOM 1601 CA GLN B 274 83.579 13.230 2.220 1.00 20.00 6 ATOM 1602 CB GLN B 274 83.176 14.322 1.222 1.00 20.00 6 ATOM 1603 CG GLN B 274 83.149 13.857 −0.230 1.00 20.00 6 ATOM 1604 CD GLN B 274 82.558 14.898 −1.169 1.00 20.00 6 ATOM 1605 OE1 GLN B 274 82.108 15.961 −0.736 1.00 20.00 8 ATOM 1606 NE2 GLN B 274 82.548 14.591 −2.462 1.00 20.00 7 ATOM 1607 C GLN B 274 85.013 12.788 1.953 1.00 20.00 6 ATOM 1608 O GLN B 274 85.239 11.818 1.233 1.00 20.00 8 ATOM 1609 N LEU B 275 85.981 13.498 2.528 1.00 20.00 7 ATOM 1610 CA LEU B 275 87.389 13.143 2.333 1.00 20.00 6 ATOM 1611 CB LEU B 275 88.311 14.194 2.971 1.00 20.00 6 ATOM 1612 CG LEU B 275 88.418 15.561 2.284 1.00 20.00 6 ATOM 1613 CD1 LEU B 275 89.325 16.481 3.088 1.00 20.00 6 ATOM 1614 CD2 LEU B 275 88.969 15.379 0.879 1.00 20.00 6 ATOM 1615 C LEU B 275 87.697 11.779 2.940 1.00 20.00 6 ATOM 1616 O LEU B 275 88.430 10.981 2.354 1.00 20.00 8 ATOM 1617 N VAL B 276 87.125 11.519 4.112 1.00 20.00 7 ATOM 1618 CA VAL B 276 87.353 10.269 4.827 1.00 20.00 6 ATOM 1619 CB VAL B 276 87.096 10.451 6.342 1.00 20.00 6 ATOM 1620 CG1 VAL B 276 87.376 9.148 7.082 1.00 20.00 6 ATOM 1621 CG2 VAL B 276 87.973 11.580 6.891 1.00 20.00 6 ATOM 1622 C VAL B 276 86.504 9.089 4.336 1.00 20.00 6 ATOM 1623 O VAL B 276 87.005 7.973 4.195 1.00 20.00 8 ATOM 1624 N ALA B 277 85.222 9.337 4.090 1.00 20.00 7 ATOM 1625 CA ALA B 277 84.310 8.291 3.643 1.00 20.00 6 ATOM 1626 CB ALA B 277 82.898 8.597 4.124 1.00 20.00 6 ATOM 1627 C ALA B 277 84.315 8.115 2.130 1.00 20.00 6 ATOM 1628 O ALA B 277 84.036 7.029 1.627 1.00 20.00 8 ATOM 1629 N GLY B 278 84.632 9.180 1.405 1.00 20.00 7 ATOM 1630 CA GLY B 278 84.653 9.099 −0.041 1.00 20.00 6 ATOM 1631 C GLY B 278 83.365 9.627 −0.644 1.00 20.00 6 ATOM 1632 O GLY B 278 83.272 9.817 −1.860 1.00 20.00 8 ATOM 1633 N LEU B 279 82.375 9.867 0.211 1.00 20.00 7 ATOM 1634 CA LEU B 279 81.075 10.382 −0.219 1.00 20.00 6 ATOM 1635 CB LEU B 279 80.070 9.232 −0.375 1.00 20.00 6 ATOM 1636 CG LEU B 279 80.342 8.114 −1.385 1.00 20.00 6 ATOM 1637 CD1 LEU B 279 79.311 7.009 −1.191 1.00 20.00 6 ATOM 1638 CD2 LEU B 279 80.291 8.660 −2.804 1.00 20.00 6 ATOM 1639 C LEU B 279 80.522 11.369 0.812 1.00 20.00 6 ATOM 1640 O LEU B 279 80.750 11.218 2.007 1.00 20.00 8 ATOM 1641 N PRO B 280 79.787 12.395 0.361 1.00 20.00 7 ATOM 1642 CD PRO B 280 79.403 12.730 −1.020 1.00 20.00 6 ATOM 1643 CA PRO B 280 79.230 13.361 1.314 1.00 20.00 6 ATOM 1644 CB PRO B 280 78.569 14.397 0.407 1.00 20.00 6 ATOM 1645 CG PRO B 280 78.191 13.598 −0.802 1.00 20.00 6 ATOM 1646 C PRO B 280 78.242 12.662 2.262 1.00 20.00 6 ATOM 1647 O PRO B 280 77.666 11.633 1.913 1.00 20.00 8 ATOM 1648 N PRO B 281 78.035 13.220 3.470 1.00 20.00 7 ATOM 1649 CD PRO B 281 78.571 14.535 3.859 1.00 20.00 6 ATOM 1650 CA PRO B 281 77.145 12.701 4.520 1.00 20.00 6 ATOM 1651 CB PRO B 281 77.262 13.746 5.634 1.00 20.00 6 ATOM 1652 CG PRO B 281 78.546 14.450 5.344 1.00 20.00 6 ATOM 1653 C PRO B 281 75.679 12.485 4.142 1.00 20.00 6 ATOM 1654 O PRO B 281 75.094 11.441 4.442 1.00 20.00 8 ATOM 1655 N PHE B 282 75.088 13.487 3.504 1.00 20.00 7 ATOM 1656 CA PHE B 282 73.686 13.427 3.123 1.00 20.00 6 ATOM 1657 CB PHE B 282 73.006 14.734 3.531 1.00 20.00 6 ATOM 1658 CG PHE B 282 73.300 15.146 4.947 1.00 20.00 6 ATOM 1659 CD1 PHE B 282 72.624 14.560 6.013 1.00 20.00 6 ATOM 1660 CD2 PHE B 282 74.295 16.085 5.218 1.00 20.00 6 ATOM 1661 CE1 PHE B 282 72.934 14.902 7.331 1.00 20.00 6 ATOM 1662 CE2 PHE B 282 74.613 16.433 6.530 1.00 20.00 6 ATOM 1663 CZ PHE B 282 73.930 15.840 7.591 1.00 20.00 6 ATOM 1664 C PHE B 282 73.527 13.191 1.628 1.00 20.00 6 ATOM 1665 O PHE B 282 73.797 14.079 0.819 1.00 20.00 8 ATOM 1666 N ARG B 283 73.080 11.994 1.267 1.00 20.00 7 ATOM 1667 CA ARG B 283 72.888 11.635 −0.134 1.00 20.00 6 ATOM 1668 CB ARG B 283 73.931 10.598 −0.559 1.00 20.00 6 ATOM 1669 CG ARG B 283 75.358 10.928 −0.151 1.00 20.00 6 ATOM 1670 CD ARG B 283 76.326 9.883 −0.687 1.00 20.00 6 ATOM 1671 NE ARG B 283 76.054 8.555 −0.142 1.00 20.00 7 ATOM 1672 CZ ARG B 283 76.404 8.159 1.077 1.00 20.00 6 ATOM 1673 NH1 ARG B 283 77.047 8.986 1.893 1.00 20.00 7 ATOM 1674 NH2 ARG B 283 76.108 6.933 1.484 1.00 20.00 7 ATOM 1675 C ARG B 283 71.493 11.046 −0.331 1.00 20.00 6 ATOM 1676 O ARG B 283 70.957 10.391 0.563 1.00 20.00 8 ATOM 1677 N ALA B 284 70.911 11.276 −1.502 1.00 20.00 7 ATOM 1678 CA ALA B 284 69.579 10.755 −1.796 1.00 20.00 6 ATOM 1679 CB ALA B 284 68.532 11.484 −0.961 1.00 20.00 6 ATOM 1680 C ALA B 284 69.278 10.921 −3.273 1.00 20.00 6 ATOM 1681 O ALA B 284 70.007 11.611 −3.984 1.00 20.00 8 ATOM 1682 N GLY B 285 68.191 10.299 −3.722 1.00 20.00 7 ATOM 1683 CA GLY B 285 67.807 10.360 −5.122 1.00 20.00 6 ATOM 1684 C GLY B 285 67.561 11.737 −5.707 1.00 20.00 6 ATOM 1685 O GLY B 285 67.775 11.955 −6.899 1.00 20.00 8 ATOM 1686 N ASN B 286 67.089 12.673 −4.892 1.00 20.00 7 ATOM 1687 CA ASN B 286 66.835 14.018 −5.386 1.00 20.00 6 ATOM 1688 CB ASN B 286 65.403 14.137 −5.930 1.00 20.00 6 ATOM 1689 CG ASN B 286 64.342 13.825 −4.885 1.00 20.00 6 ATOM 1690 OD1 ASN B 286 64.292 14.450 −3.826 1.00 20.00 8 ATOM 1691 ND2 ASN B 286 63.477 12.861 −5.190 1.00 20.00 7 ATOM 1692 C ASN B 286 67.076 15.042 −4.291 1.00 20.00 6 ATOM 1693 O ASN B 286 67.368 14.682 −3.152 1.00 20.00 8 ATOM 1694 N GLU B 287 66.955 16.317 −4.636 1.00 20.00 7 ATOM 1695 CA GLU B 287 67.185 17.377 −3.669 1.00 20.00 6 ATOM 1696 CB GLU B 287 67.181 18.738 −4.365 1.00 20.00 6 ATOM 1697 CG GLU B 287 68.537 19.095 −4.944 1.00 20.00 6 ATOM 1698 CD GLU B 287 68.524 20.385 −5.735 1.00 20.00 6 ATOM 1699 OE1 GLU B 287 67.911 21.371 −5.267 1.00 20.00 8 ATOM 1700 OE2 GLU B 287 69.144 20.410 −6.823 1.00 20.00 8 ATOM 1701 C GLU B 287 66.225 17.394 −2.492 1.00 20.00 6 ATOM 1702 O GLU B 287 66.658 17.554 −1.354 1.00 20.00 8 ATOM 1703 N TYR B 288 64.932 17.233 −2.753 1.00 20.00 7 ATOM 1704 CA TYR B 288 63.955 17.239 −1.670 1.00 20.00 6 ATOM 1705 CB TYR B 288 62.553 16.899 −2.184 1.00 20.00 6 ATOM 1706 CG TYR B 288 61.530 16.780 −1.070 1.00 20.00 6 ATOM 1707 CD1 TYR B 288 60.984 17.917 −0.470 1.00 20.00 6 ATOM 1708 CE1 TYR B 288 60.090 17.814 0.600 1.00 20.00 6 ATOM 1709 CD2 TYR B 288 61.154 15.529 −0.573 1.00 20.00 6 ATOM 1710 CE2 TYR B 288 60.265 15.414 0.498 1.00 20.00 6 ATOM 1711 CZ TYR B 288 59.740 16.561 1.078 1.00 20.00 6 ATOM 1712 OH TYR B 288 58.884 16.454 2.149 1.00 20.00 8 ATOM 1713 C TYR B 288 64.337 16.238 −0.587 1.00 20.00 6 ATOM 1714 O TYR B 288 64.254 16.545 0.598 1.00 20.00 8 ATOM 1715 N LEU B 289 64.750 15.041 −1.001 1.00 20.00 7 ATOM 1716 CA LEU B 289 65.137 13.989 −0.064 1.00 20.00 6 ATOM 1717 CB LEU B 289 65.283 12.649 −0.797 1.00 20.00 6 ATOM 1718 CG LEU B 289 63.984 11.985 −1.274 1.00 20.00 6 ATOM 1719 CD1 LEU B 289 64.314 10.802 −2.179 1.00 20.00 6 ATOM 1720 CD2 LEU B 289 63.160 11.530 −0.068 1.00 20.00 6 ATOM 1721 C LEU B 289 66.431 14.310 0.685 1.00 20.00 6 ATOM 1722 O LEU B 289 66.604 13.914 1.840 1.00 20.00 8 ATOM 1723 N ILE B 290 67.340 15.017 0.025 1.00 20.00 7 ATOM 1724 CA ILE B 290 68.597 15.390 0.658 1.00 20.00 6 ATOM 1725 CB ILE B 290 69.583 15.985 −0.366 1.00 20.00 6 ATOM 1726 CG2 ILE B 290 70.778 16.609 0.359 1.00 20.00 6 ATOM 1727 CG1 ILE B 290 70.046 14.887 −1.330 1.00 20.00 6 ATOM 1728 CD1 ILE B 290 70.844 15.398 −2.518 1.00 20.00 6 ATOM 1729 C ILE B 290 68.307 16.424 1.743 1.00 20.00 6 ATOM 1730 O ILE B 290 68.807 16.317 2.862 1.00 20.00 8 ATOM 1731 N PHE B 291 67.491 17.420 1.411 1.00 20.00 7 ATOM 1732 CA PHE B 291 67.143 18.462 2.372 1.00 20.00 6 ATOM 1733 CB PHE B 291 66.222 19.502 1.731 1.00 20.00 6 ATOM 1734 CG PHE B 291 66.869 20.289 0.628 1.00 20.00 6 ATOM 1735 CD1 PHE B 291 68.255 20.420 0.568 1.00 20.00 6 ATOM 1736 CD2 PHE B 291 66.094 20.931 −0.332 1.00 20.00 6 ATOM 1737 CE1 PHE B 291 68.859 21.182 −0.435 1.00 20.00 6 ATOM 1738 CE2 PHE B 291 66.690 21.697 −1.340 1.00 20.00 6 ATOM 1739 CZ PHE B 291 68.074 21.822 −1.390 1.00 20.00 6 ATOM 1740 C PHE B 291 66.453 17.848 3.576 1.00 20.00 6 ATOM 1741 O PHE B 291 66.664 18.262 4.718 1.00 20.00 8 ATOM 1742 N GLN B 292 65.629 16.847 3.303 1.00 20.00 7 ATOM 1743 CA GLN B 292 64.887 16.154 4.341 1.00 20.00 6 ATOM 1744 CB GLN B 292 64.006 15.090 3.687 1.00 20.00 6 ATOM 1745 CG GLN B 292 62.953 14.486 4.572 1.00 20.00 6 ATOM 1746 CD GLN B 292 61.895 13.750 3.763 1.00 20.00 6 ATOM 1747 OE1 GLN B 292 62.208 12.835 2.997 1.00 20.00 8 ATOM 1748 NE2 GLN B 292 60.637 14.155 3.924 1.00 20.00 7 ATOM 1749 C GLN B 292 65.865 15.522 5.329 1.00 20.00 6 ATOM 1750 O GLN B 292 65.689 15.630 6.540 1.00 20.00 8 ATOM 1751 N LYS B 293 66.907 14.875 4.812 1.00 20.00 7 ATOM 1752 CA LYS B 293 67.898 14.244 5.683 1.00 20.00 6 ATOM 1753 CB LYS B 293 68.850 13.372 4.865 1.00 20.00 6 ATOM 1754 CG LYS B 293 68.197 12.135 4.278 1.00 20.00 6 ATOM 1755 CD LYS B 293 69.217 11.260 3.554 1.00 20.00 6 ATOM 1756 CE LYS B 293 68.575 9.972 3.051 1.00 20.00 6 ATOM 1757 NZ LYS B 293 69.553 9.099 2.339 1.00 20.00 7 ATOM 1758 C LYS B 293 68.698 15.287 6.468 1.00 20.00 6 ATOM 1759 O LYS B 293 69.044 15.074 7.634 1.00 20.00 8 ATOM 1760 N ILE B 294 68.989 16.411 5.827 1.00 20.00 7 ATOM 1761 CA ILE B 294 69.745 17.480 6.472 1.00 20.00 6 ATOM 1762 CB ILE B 294 70.026 18.632 5.474 1.00 20.00 6 ATOM 1763 CG2 ILE B 294 70.489 19.881 6.223 1.00 20.00 6 ATOM 1764 CG1 ILE B 294 71.070 18.178 4.443 1.00 20.00 6 ATOM 1765 CD1 ILE B 294 71.266 19.159 3.303 1.00 20.00 6 ATOM 1766 C ILE B 294 69.035 18.045 7.712 1.00 20.00 6 ATOM 1767 O ILE B 294 69.618 18.091 8.798 1.00 20.00 8 ATOM 1768 N ILE B 295 67.783 18.467 7.564 1.00 20.00 7 ATOM 1769 CA ILE B 295 67.068 19.037 8.707 1.00 20.00 6 ATOM 1770 CB ILE B 295 65.710 19.647 8.300 1.00 20.00 6 ATOM 1771 CG2 ILE B 295 65.927 20.749 7.265 1.00 20.00 6 ATOM 1772 CG1 ILE B 295 64.784 18.559 7.762 1.00 20.00 6 ATOM 1773 CD1 ILE B 295 63.356 19.037 7.558 1.00 20.00 6 ATOM 1774 C ILE B 295 66.831 18.045 9.842 1.00 20.00 6 ATOM 1775 O ILE B 295 66.540 18.447 10.967 1.00 20.00 8 ATOM 1776 N LYS B 296 66.956 16.753 9.550 1.00 20.00 7 ATOM 1777 CA LYS B 296 66.765 15.724 10.569 1.00 20.00 6 ATOM 1778 CB LYS B 296 65.907 14.576 10.019 1.00 20.00 6 ATOM 1779 CG LYS B 296 64.535 15.010 9.538 1.00 20.00 6 ATOM 1780 CD LYS B 296 63.739 13.851 8.951 1.00 20.00 6 ATOM 1781 CE LYS B 296 63.296 12.873 10.025 1.00 20.00 6 ATOM 1782 NZ LYS B 296 62.375 11.828 9.482 1.00 20.00 7 ATOM 1783 C LYS B 296 68.116 15.176 11.018 1.00 20.00 6 ATOM 1784 O LYS B 296 68.178 14.261 11.838 1.00 20.00 8 ATOM 1785 N LEU B 297 69.190 15.746 10.474 1.00 20.00 7 ATOM 1786 CA LEU B 297 70.551 15.320 10.791 1.00 20.00 6 ATOM 1787 CB LEU B 297 70.911 15.680 12.236 1.00 20.00 6 ATOM 1788 CG LEU B 297 72.398 15.538 12.585 1.00 20.00 6 ATOM 1789 CD1 LEU B 297 73.215 16.555 11.771 1.00 20.00 6 ATOM 1790 CD2 LEU B 297 72.605 15.762 14.076 1.00 20.00 6 ATOM 1791 C LEU B 297 70.635 13.810 10.592 1.00 20.00 6 ATOM 1792 O LEU B 297 71.150 13.080 11.434 1.00 20.00 8 ATOM 1793 N GLU B 298 70.128 13.351 9.456 1.00 20.00 7 ATOM 1794 CA GLU B 298 70.115 11.934 9.148 1.00 20.00 6 ATOM 1795 CB GLU B 298 68.817 11.597 8.416 1.00 20.00 6 ATOM 1796 CG GLU B 298 68.568 10.123 8.233 1.00 20.00 6 ATOM 1797 CD GLU B 298 67.254 9.858 7.535 1.00 20.00 6 ATOM 1798 OE1 GLU B 298 66.214 10.331 8.043 1.00 20.00 8 ATOM 1799 OE2 GLU B 298 67.261 9.185 6.484 1.00 20.00 8 ATOM 1800 C GLU B 298 71.309 11.446 8.332 1.00 20.00 6 ATOM 1801 O GLU B 298 71.310 11.523 7.104 1.00 20.00 8 ATOM 1802 N TYR B 299 72.325 10.946 9.027 1.00 20.00 7 ATOM 1803 CA TYR B 299 73.519 10.405 8.390 1.00 20.00 6 ATOM 1804 CB TYR B 299 74.444 11.521 7.880 1.00 20.00 6 ATOM 1805 CG TYR B 299 75.330 12.130 8.953 1.00 20.00 6 ATOM 1806 CD1 TYR B 299 74.796 12.962 9.935 1.00 20.00 6 ATOM 1807 CE1 TYR B 299 75.589 13.482 10.951 1.00 20.00 6 ATOM 1808 CD2 TYR B 299 76.692 11.833 9.013 1.00 20.00 6 ATOM 1809 CE2 TYR B 299 77.499 12.352 10.032 1.00 20.00 6 ATOM 1810 CZ TYR B 299 76.935 13.173 10.995 1.00 20.00 6 ATOM 1811 OH TYR B 299 77.701 13.687 12.006 1.00 20.00 8 ATOM 1812 C TYR B 299 74.245 9.600 9.456 1.00 20.00 6 ATOM 1813 O TYR B 299 73.913 9.688 10.631 1.00 20.00 8 ATOM 1814 N ASP B 300 75.229 8.808 9.052 1.00 20.00 7 ATOM 1815 CA ASP B 300 75.991 8.030 10.016 1.00 20.00 6 ATOM 1816 CB ASP B 300 75.291 6.700 10.304 1.00 20.00 6 ATOM 1817 CG ASP B 300 74.898 5.968 9.048 1.00 20.00 6 ATOM 1818 OD1 ASP B 300 75.806 5.594 8.274 1.00 20.00 8 ATOM 1819 OD2 ASP B 300 73.681 5.771 8.832 1.00 20.00 8 ATOM 1820 C ASP B 300 77.397 7.799 9.488 1.00 20.00 6 ATOM 1821 O ASP B 300 77.651 7.976 8.297 1.00 20.00 8 ATOM 1822 N PHE B 301 78.307 7.417 10.378 1.00 20.00 7 ATOM 1823 CA PHE B 301 79.695 7.186 9.996 1.00 20.00 6 ATOM 1824 CB PHE B 301 80.655 7.664 11.093 1.00 20.00 6 ATOM 1825 CG PHE B 301 80.488 9.103 11.481 1.00 20.00 6 ATOM 1826 CD1 PHE B 301 79.493 9.487 12.370 1.00 20.00 6 ATOM 1827 CD2 PHE B 301 81.346 10.075 10.970 1.00 20.00 6 ATOM 1828 CE1 PHE B 301 79.352 10.823 12.750 1.00 20.00 6 ATOM 1829 CE2 PHE B 301 81.214 11.408 11.342 1.00 20.00 6 ATOM 1830 CZ PHE B 301 80.215 11.783 12.235 1.00 20.00 6 ATOM 1831 C PHE B 301 80.009 5.722 9.744 1.00 20.00 6 ATOM 1832 O PHE B 301 79.506 4.839 10.442 1.00 20.00 8 ATOM 1833 N PRO B 302 80.842 5.440 8.732 1.00 20.00 7 ATOM 1834 CD PRO B 302 81.330 6.316 7.654 1.00 20.00 6 ATOM 1835 CA PRO B 302 81.191 4.044 8.466 1.00 20.00 6 ATOM 1836 CB PRO B 302 81.838 4.105 7.084 1.00 20.00 6 ATOM 1837 CG PRO B 302 82.425 5.479 7.046 1.00 20.00 6 ATOM 1838 C PRO B 302 82.168 3.629 9.569 1.00 20.00 6 ATOM 1839 O PRO B 302 82.887 4.469 10.111 1.00 20.00 8 ATOM 1840 N ALA B 303 82.185 2.345 9.908 1.00 20.00 7 ATOM 1841 CA ALA B 303 83.052 1.836 10.968 1.00 20.00 6 ATOM 1842 CB ALA B 303 82.993 0.310 10.987 1.00 20.00 6 ATOM 1843 C ALA B 303 84.513 2.294 10.939 1.00 20.00 6 ATOM 1844 O ALA B 303 85.078 2.637 11.979 1.00 20.00 8 ATOM 1845 N ALA B 304 85.121 2.306 9.756 1.00 20.00 7 ATOM 1846 CA ALA B 304 86.527 2.684 9.605 1.00 20.00 6 ATOM 1847 CB ALA B 304 86.971 2.423 8.165 1.00 20.00 6 ATOM 1848 C ALA B 304 86.894 4.119 10.001 1.00 20.00 6 ATOM 1849 O ALA B 304 87.983 4.367 10.520 1.00 20.00 8 ATOM 1850 N PHE B 305 85.985 5.053 9.742 1.00 20.00 7 ATOM 1851 CA PHE B 305 86.183 6.473 10.034 1.00 20.00 6 ATOM 1852 CB PHE B 305 84.822 7.115 10.312 1.00 20.00 6 ATOM 1853 CG PHE B 305 84.705 8.522 9.815 1.00 20.00 6 ATOM 1854 CD1 PHE B 305 85.303 9.572 10.502 1.00 20.00 6 ATOM 1855 CD2 PHE B 305 84.003 8.800 8.646 1.00 20.00 6 ATOM 1856 CE1 PHE B 305 85.202 10.881 10.033 1.00 20.00 6 ATOM 1857 CE2 PHE B 305 83.896 10.106 8.167 1.00 20.00 6 ATOM 1858 CZ PHE B 305 84.496 11.147 8.862 1.00 20.00 6 ATOM 1859 C PHE B 305 87.153 6.789 11.182 1.00 20.00 6 ATOM 1860 O PHE B 305 86.964 6.342 12.312 1.00 20.00 8 ATOM 1861 N PHE B 306 88.190 7.565 10.883 1.00 20.00 7 ATOM 1862 CA PHE B 306 89.176 7.945 11.894 1.00 20.00 6 ATOM 1863 CB PHE B 306 90.179 8.936 11.295 1.00 20.00 6 ATOM 1864 CG PHE B 306 90.695 8.531 9.940 1.00 20.00 6 ATOM 1865 CD1 PHE B 306 91.292 7.284 9.747 1.00 20.00 6 ATOM 1866 CD2 PHE B 306 90.588 9.395 8.853 1.00 20.00 6 ATOM 1867 CE1 PHE B 306 91.774 6.906 8.490 1.00 20.00 6 ATOM 1868 CE2 PHE B 306 91.067 9.027 7.590 1.00 20.00 6 ATOM 1869 CZ PHE B 306 91.662 7.780 7.408 1.00 20.00 6 ATOM 1870 C PHE B 306 88.445 8.575 13.086 1.00 20.00 6 ATOM 1871 O PHE B 306 87.731 9.566 12.936 1.00 20.00 8 ATOM 1872 N PRO B 307 88.614 7.995 14.288 1.00 20.00 7 ATOM 1873 CD PRO B 307 89.482 6.834 14.555 1.00 20.00 6 ATOM 1874 CA PRO B 307 87.983 8.459 15.530 1.00 20.00 6 ATOM 1875 CB PRO B 307 88.748 7.691 16.606 1.00 20.00 6 ATOM 1876 CG PRO B 307 89.018 6.388 15.928 1.00 20.00 6 ATOM 1877 C PRO B 307 87.986 9.965 15.784 1.00 20.00 6 ATOM 1878 O PRO B 307 86.936 10.565 16.025 1.00 20.00 8 ATOM 1879 N LYS B 308 89.162 10.575 15.745 1.00 20.00 7 ATOM 1880 CA LYS B 308 89.260 12.004 15.992 1.00 20.00 6 ATOM 1881 CB LYS B 308 90.728 12.405 16.149 1.00 20.00 6 ATOM 1882 CG LYS B 308 91.338 11.805 17.410 1.00 20.00 6 ATOM 1883 CD LYS B 308 92.806 12.140 17.591 1.00 20.00 6 ATOM 1884 CE LYS B 308 93.339 11.457 18.847 1.00 20.00 6 ATOM 1885 NZ LYS B 308 94.816 11.573 18.985 1.00 20.00 7 ATOM 1886 C LYS B 308 88.572 12.808 14.894 1.00 20.00 6 ATOM 1887 O LYS B 308 87.985 13.855 15.167 1.00 20.00 8 ATOM 1888 N ALA B 309 88.629 12.318 13.659 1.00 20.00 7 ATOM 1889 CA ALA B 309 87.967 13.011 12.557 1.00 20.00 6 ATOM 1890 CB ALA B 309 88.328 12.369 11.231 1.00 20.00 6 ATOM 1891 C ALA B 309 86.460 12.936 12.787 1.00 20.00 6 ATOM 1892 O ALA B 309 85.735 13.903 12.552 1.00 20.00 8 ATOM 1893 N ARG B 310 85.986 11.780 13.246 1.00 20.00 7 ATOM 1894 CA ARG B 310 84.561 11.619 13.513 1.00 20.00 6 ATOM 1895 CB ARG B 310 84.246 10.194 13.979 1.00 20.00 6 ATOM 1896 CG ARG B 310 82.844 10.069 14.561 1.00 20.00 6 ATOM 1897 CD ARG B 310 82.408 8.632 14.789 1.00 20.00 6 ATOM 1898 NE ARG B 310 81.060 8.593 15.355 1.00 20.00 7 ATOM 1899 CZ ARG B 310 80.259 7.532 15.328 1.00 20.00 6 ATOM 1900 NH1 ARG B 310 80.665 6.401 14.759 1.00 20.00 7 ATOM 1901 NH2 ARG B 310 79.048 7.601 15.867 1.00 20.00 7 ATOM 1902 C ARG B 310 84.110 12.613 14.583 1.00 20.00 6 ATOM 1903 O ARG B 310 83.080 13.274 14.436 1.00 20.00 8 ATOM 1904 N ASP B 311 84.876 12.707 15.666 1.00 20.00 7 ATOM 1905 CA ASP B 311 84.535 13.629 16.740 1.00 20.00 6 ATOM 1906 CB ASP B 311 85.574 13.555 17.864 1.00 20.00 6 ATOM 1907 CG ASP B 311 85.260 14.505 19.006 1.00 20.00 6 ATOM 1908 OD1 ASP B 311 85.782 15.636 19.010 1.00 20.00 8 ATOM 1909 OD2 ASP B 311 84.480 14.124 19.901 1.00 20.00 8 ATOM 1910 C ASP B 311 84.445 15.054 16.198 1.00 20.00 6 ATOM 1911 O ASP B 311 83.539 15.800 16.564 1.00 20.00 8 ATOM 1912 N LEU B 312 85.371 15.423 15.313 1.00 20.00 7 ATOM 1913 CA LEU B 312 85.362 16.769 14.736 1.00 20.00 6 ATOM 1914 CB LEU B 312 86.604 16.999 13.869 1.00 20.00 6 ATOM 1915 CG LEU B 312 86.662 18.329 13.099 1.00 20.00 6 ATOM 1916 CD1 LEU B 312 86.424 19.510 14.037 1.00 20.00 6 ATOM 1917 CD2 LEU B 312 88.018 18.450 12.414 1.00 20.00 6 ATOM 1918 C LEU B 312 84.112 17.008 13.899 1.00 20.00 6 ATOM 1919 O LEU B 312 83.456 18.039 14.035 1.00 20.00 8 ATOM 1920 N VAL B 313 83.786 16.051 13.033 1.00 20.00 7 ATOM 1921 CA VAL B 313 82.611 16.171 12.183 1.00 20.00 6 ATOM 1922 CB VAL B 313 82.464 14.942 11.255 1.00 20.00 6 ATOM 1923 CG1 VAL B 313 81.121 14.973 10.551 1.00 20.00 6 ATOM 1924 CG2 VAL B 313 83.595 14.935 10.228 1.00 20.00 6 ATOM 1925 C VAL B 313 81.354 16.315 13.036 1.00 20.00 6 ATOM 1926 O VAL B 313 80.467 17.111 12.716 1.00 20.00 8 ATOM 1927 N GLU B 314 81.282 15.559 14.129 1.00 20.00 7 ATOM 1928 CA GLU B 314 80.122 15.634 15.010 1.00 20.00 6 ATOM 1929 CB GLU B 314 80.191 14.545 16.084 1.00 20.00 6 ATOM 1930 CG GLU B 314 80.160 13.131 15.521 1.00 20.00 6 ATOM 1931 CD GLU B 314 80.222 12.073 16.603 1.00 20.00 6 ATOM 1932 OE1 GLU B 314 81.033 12.227 17.542 1.00 20.00 8 ATOM 1933 OE2 GLU B 314 79.469 11.081 16.512 1.00 20.00 8 ATOM 1934 C GLU B 314 80.035 17.005 15.664 1.00 20.00 6 ATOM 1935 O GLU B 314 78.960 17.443 16.059 1.00 20.00 8 ATOM 1936 N LYS B 315 81.165 17.690 15.776 1.00 20.00 7 ATOM 1937 CA LYS B 315 81.154 19.010 16.383 1.00 20.00 6 ATOM 1938 CB LYS B 315 82.448 19.240 17.168 1.00 20.00 6 ATOM 1939 CG LYS B 315 82.460 18.478 18.493 1.00 20.00 6 ATOM 1940 CD LYS B 315 83.803 18.529 19.198 1.00 20.00 6 ATOM 1941 CE LYS B 315 83.749 17.825 20.552 1.00 20.00 6 ATOM 1942 NZ LYS B 315 82.829 18.505 21.506 1.00 20.00 7 ATOM 1943 C LYS B 315 80.934 20.104 15.343 1.00 20.00 6 ATOM 1944 O LYS B 315 80.855 21.282 15.686 1.00 20.00 8 ATOM 1945 N LEU B 316 80.819 19.706 14.075 1.00 20.00 7 ATOM 1946 CA LEU B 316 80.577 20.649 12.979 1.00 20.00 6 ATOM 1947 CB LEU B 316 81.608 20.450 11.863 1.00 20.00 6 ATOM 1948 CG LEU B 316 83.044 20.833 12.240 1.00 20.00 6 ATOM 1949 CD1 LEU B 316 84.011 20.365 11.156 1.00 20.00 6 ATOM 1950 CD2 LEU B 316 83.124 22.351 12.434 1.00 20.00 6 ATOM 1951 C LEU B 316 79.164 20.469 12.415 1.00 20.00 6 ATOM 1952 O LEU B 316 78.464 21.448 12.148 1.00 20.00 8 ATOM 1953 N LEU B 317 78.746 19.220 12.230 1.00 20.00 7 ATOM 1954 CA LEU B 317 77.403 18.962 11.721 1.00 20.00 6 ATOM 1955 CB LEU B 317 77.343 17.605 11.012 1.00 20.00 6 ATOM 1956 CG LEU B 317 78.335 17.445 9.852 1.00 20.00 6 ATOM 1957 CD1 LEU B 317 78.091 16.111 9.143 1.00 20.00 6 ATOM 1958 CD2 LEU B 317 78.182 18.603 8.866 1.00 20.00 6 ATOM 1959 C LEU B 317 76.435 19.000 12.899 1.00 20.00 6 ATOM 1960 O LEU B 317 75.979 17.966 13.398 1.00 20.00 8 ATOM 1961 N VAL B 318 76.156 20.215 13.354 1.00 20.00 7 ATOM 1962 CA VAL B 318 75.251 20.451 14.467 1.00 20.00 6 ATOM 1963 CB VAL B 318 75.981 21.164 15.625 1.00 20.00 6 ATOM 1964 CG1 VAL B 318 75.007 21.461 16.759 1.00 20.00 6 ATOM 1965 CG2 VAL B 318 77.136 20.300 16.115 1.00 20.00 6 ATOM 1966 C VAL B 318 74.140 21.344 13.936 1.00 20.00 6 ATOM 1967 O VAL B 318 74.410 22.386 13.333 1.00 20.00 8 ATOM 1968 N LEU B 319 72.892 20.941 14.153 1.00 20.00 7 ATOM 1969 CA LEU B 319 71.758 21.717 13.663 1.00 20.00 6 ATOM 1970 CB LEU B 319 70.444 21.056 14.093 1.00 20.00 6 ATOM 1971 CG LEU B 319 70.211 19.647 13.533 1.00 20.00 6 ATOM 1972 CD1 LEU B 319 68.883 19.098 14.060 1.00 20.00 6 ATOM 1973 CD2 LEU B 319 70.211 19.688 12.000 1.00 20.00 6 ATOM 1974 C LEU B 319 71.794 23.173 14.119 1.00 20.00 6 ATOM 1975 O LEU B 319 71.591 24.082 13.317 1.00 20.00 8 ATOM 1976 N ASP B 320 72.052 23.394 15.405 1.00 20.00 7 ATOM 1977 CA ASP B 320 72.119 24.745 15.958 1.00 20.00 6 ATOM 1978 CB ASP B 320 72.091 24.687 17.490 1.00 20.00 6 ATOM 1979 CG ASP B 320 72.058 26.061 18.129 1.00 20.00 6 ATOM 1980 OD1 ASP B 320 72.506 27.036 17.492 1.00 20.00 8 ATOM 1981 OD2 ASP B 320 71.595 26.166 19.284 1.00 20.00 8 ATOM 1982 C ASP B 320 73.415 25.419 15.492 1.00 20.00 6 ATOM 1983 O ASP B 320 74.496 25.089 15.965 1.00 20.00 8 ATOM 1984 N ALA B 321 73.294 26.372 14.576 1.00 20.00 7 ATOM 1985 CA ALA B 321 74.450 27.078 14.028 1.00 20.00 6 ATOM 1986 CB ALA B 321 73.982 28.109 13.006 1.00 20.00 6 ATOM 1987 C ALA B 321 75.359 27.747 15.065 1.00 20.00 6 ATOM 1988 O ALA B 321 76.535 27.992 14.790 1.00 20.00 8 ATOM 1989 N THR B 322 74.829 28.035 16.252 1.00 20.00 7 ATOM 1990 CA THR B 322 75.631 28.681 17.292 1.00 20.00 6 ATOM 1991 CB THR B 322 74.755 29.491 18.271 1.00 20.00 6 ATOM 1992 OG1 THR B 322 73.879 28.605 18.973 1.00 20.00 8 ATOM 1993 CG2 THR B 322 73.928 30.527 17.519 1.00 20.00 6 ATOM 1994 C THR B 322 76.437 27.684 18.108 1.00 20.00 6 ATOM 1995 O THR B 322 77.166 28.071 19.019 1.00 20.00 8 ATOM 1996 N LYS B 323 76.312 26.401 17.786 1.00 20.00 7 ATOM 1997 CA LYS B 323 77.048 25.378 18.517 1.00 20.00 6 ATOM 1998 CB LYS B 323 76.080 24.378 19.155 1.00 20.00 6 ATOM 1999 CG LYS B 323 75.180 24.992 20.209 1.00 20.00 6 ATOM 2000 CD LYS B 323 74.356 23.931 20.924 1.00 20.00 6 ATOM 2001 CE LYS B 323 73.406 24.574 21.927 1.00 20.00 6 ATOM 2002 NZ LYS B 323 74.144 25.514 22.818 1.00 20.00 7 ATOM 2003 C LYS B 323 78.066 24.631 17.664 1.00 20.00 6 ATOM 2004 O LYS B 323 78.520 23.557 18.040 1.00 20.00 8 ATOM 2005 N ARG B 324 78.427 25.195 16.517 1.00 20.00 7 ATOM 2006 CA ARG B 324 79.408 24.545 15.656 1.00 20.00 6 ATOM 2007 CB ARG B 324 79.108 24.834 14.186 1.00 20.00 6 ATOM 2008 CG ARG B 324 77.824 24.177 13.728 1.00 20.00 6 ATOM 2009 CD ARG B 324 77.468 24.505 12.297 1.00 20.00 6 ATOM 2010 NE ARG B 324 76.060 24.202 12.069 1.00 20.00 7 ATOM 2011 CZ ARG B 324 75.277 24.873 11.233 1.00 20.00 6 ATOM 2012 NH1 ARG B 324 75.764 25.888 10.523 1.00 20.00 7 ATOM 2013 NH2 ARG B 324 73.992 24.551 11.140 1.00 20.00 7 ATOM 2014 C ARG B 324 80.811 25.011 16.008 1.00 20.00 6 ATOM 2015 O ARG B 324 81.070 26.212 16.131 1.00 20.00 8 ATOM 2016 N LEU B 325 81.711 24.049 16.180 1.00 20.00 7 ATOM 2017 CA LEU B 325 83.090 24.350 16.520 1.00 20.00 6 ATOM 2018 CB LEU B 325 83.913 23.061 16.550 1.00 20.00 6 ATOM 2019 CG LEU B 325 85.274 23.123 17.241 1.00 20.00 6 ATOM 2020 CD1 LEU B 325 85.093 23.591 18.682 1.00 20.00 6 ATOM 2021 CD2 LEU B 325 85.922 21.741 17.209 1.00 20.00 6 ATOM 2022 C LEU B 325 83.656 25.310 15.481 1.00 20.00 6 ATOM 2023 O LEU B 325 83.649 25.015 14.282 1.00 20.00 8 ATOM 2024 N GLY B 326 84.139 26.461 15.946 1.00 20.00 7 ATOM 2025 CA GLY B 326 84.697 27.449 15.040 1.00 20.00 6 ATOM 2026 C GLY B 326 83.857 28.711 14.932 1.00 20.00 6 ATOM 2027 O GLY B 326 84.369 29.757 14.529 1.00 20.00 8 ATOM 2028 N CYS B 327 82.575 28.632 15.286 1.00 20.00 7 ATOM 2029 CA CYS B 327 81.714 29.806 15.200 1.00 20.00 6 ATOM 2030 CB CYS B 327 80.233 29.404 15.183 1.00 20.00 6 ATOM 2031 SG CYS B 327 79.534 28.915 16.774 1.00 20.00 16 ATOM 2032 C CYS B 327 81.976 30.772 16.353 1.00 20.00 6 ATOM 2033 O CYS B 327 82.565 30.410 17.371 1.00 20.00 8 ATOM 2034 N GLU B 328 81.523 32.005 16.178 1.00 20.00 7 ATOM 2035 CA GLU B 328 81.714 33.052 17.167 1.00 20.00 6 ATOM 2036 CB GLU B 328 81.087 34.348 16.632 1.00 20.00 6 ATOM 2037 CG GLU B 328 81.734 34.772 15.300 1.00 20.00 6 ATOM 2038 CD GLU B 328 80.962 35.842 14.539 1.00 20.00 6 ATOM 2039 OE1 GLU B 328 79.738 35.676 14.343 1.00 20.00 8 ATOM 2040 OE2 GLU B 328 81.588 36.840 14.116 1.00 20.00 8 ATOM 2041 C GLU B 328 81.187 32.701 18.560 1.00 20.00 6 ATOM 2042 O GLU B 328 81.850 32.983 19.562 1.00 20.00 8 ATOM 2043 N GLU B 329 80.016 32.073 18.631 1.00 20.00 7 ATOM 2044 CA GLU B 329 79.449 31.714 19.926 1.00 20.00 6 ATOM 2045 CB GLU B 329 77.991 31.263 19.782 1.00 20.00 6 ATOM 2046 CG GLU B 329 77.028 32.355 19.315 1.00 20.00 6 ATOM 2047 CD GLU B 329 77.055 32.575 17.813 1.00 20.00 6 ATOM 2048 OE1 GLU B 329 77.859 31.910 17.120 1.00 20.00 8 ATOM 2049 OE2 GLU B 329 76.267 33.413 17.323 1.00 20.00 8 ATOM 2050 C GLU B 329 80.264 30.616 20.605 1.00 20.00 6 ATOM 2051 O GLU B 329 80.182 30.436 21.819 1.00 20.00 8 ATOM 2052 N MET B 330 81.040 29.878 19.816 1.00 20.00 7 ATOM 2053 CA MET B 330 81.880 28.813 20.354 1.00 20.00 6 ATOM 2054 CB MET B 330 81.872 27.600 19.419 1.00 20.00 6 ATOM 2055 CG MET B 330 80.552 26.822 19.436 1.00 20.00 6 ATOM 2056 SD MET B 330 80.117 26.254 21.104 1.00 20.00 16 ATOM 2057 CE MET B 330 81.265 24.895 21.311 1.00 20.00 6 ATOM 2058 C MET B 330 83.302 29.330 20.547 1.00 20.00 6 ATOM 2059 O MET B 330 84.236 28.564 20.754 1.00 20.00 8 ATOM 2060 N GLU B 331 83.443 30.647 20.471 1.00 20.00 7 ATOM 2061 CA GLU B 331 84.716 31.338 20.656 1.00 20.00 6 ATOM 2062 CB GLU B 331 85.357 30.921 21.987 1.00 20.00 6 ATOM 2063 CG GLU B 331 84.371 30.886 23.163 1.00 20.00 6 ATOM 2064 CD GLU B 331 83.478 32.127 23.270 1.00 20.00 6 ATOM 2065 OE1 GLU B 331 82.483 32.064 24.021 1.00 20.00 8 ATOM 2066 OE2 GLU B 331 83.759 33.159 22.625 1.00 20.00 8 ATOM 2067 C GLU B 331 85.742 31.247 19.523 1.00 20.00 6 ATOM 2068 O GLU B 331 86.952 31.264 19.761 1.00 20.00 8 ATOM 2069 N GLY B 332 85.257 31.137 18.292 1.00 20.00 7 ATOM 2070 CA GLY B 332 86.145 31.159 17.140 1.00 20.00 6 ATOM 2071 C GLY B 332 87.036 30.014 16.721 1.00 20.00 6 ATOM 2072 O GLY B 332 86.881 28.863 17.142 1.00 20.00 8 ATOM 2073 N TYR B 333 88.002 30.366 15.875 1.00 20.00 7 ATOM 2074 CA TYR B 333 88.939 29.413 15.307 1.00 20.00 6 ATOM 2075 CB TYR B 333 89.625 30.053 14.093 1.00 20.00 6 ATOM 2076 CG TYR B 333 88.724 30.031 12.877 1.00 20.00 6 ATOM 2077 CD1 TYR B 333 88.774 28.966 11.974 1.00 20.00 6 ATOM 2078 CE1 TYR B 333 87.872 28.869 10.919 1.00 20.00 6 ATOM 2079 CD2 TYR B 333 87.747 31.011 12.686 1.00 20.00 6 ATOM 2080 CE2 TYR B 333 86.831 30.923 11.624 1.00 20.00 6 ATOM 2081 CZ TYR B 333 86.903 29.845 10.751 1.00 20.00 6 ATOM 2082 OH TYR B 333 86.001 29.719 9.724 1.00 20.00 8 ATOM 2083 C TYR B 333 89.958 28.800 16.252 1.00 20.00 6 ATOM 2084 O TYR B 333 90.473 27.721 15.971 1.00 20.00 8 ATOM 2085 N GLY B 334 90.242 29.469 17.369 1.00 20.00 7 ATOM 2086 CA GLY B 334 91.193 28.921 18.327 1.00 20.00 6 ATOM 2087 C GLY B 334 90.803 27.504 18.741 1.00 20.00 6 ATOM 2088 O GLY B 334 91.577 26.564 18.558 1.00 20.00 8 ATOM 2089 N PRO B 335 89.603 27.320 19.309 1.00 20.00 7 ATOM 2090 CD PRO B 335 88.703 28.372 19.814 1.00 20.00 6 ATOM 2091 CA PRO B 335 89.145 25.991 19.731 1.00 20.00 6 ATOM 2092 CB PRO B 335 87.759 26.275 20.303 1.00 20.00 6 ATOM 2093 CG PRO B 335 87.925 27.644 20.883 1.00 20.00 6 ATOM 2094 C PRO B 335 89.104 24.986 18.573 1.00 20.00 6 ATOM 2095 O PRO B 335 89.406 23.808 18.756 1.00 20.00 8 ATOM 2096 N LEU B 336 88.727 25.450 17.382 1.00 20.00 7 ATOM 2097 CA LEU B 336 88.666 24.567 16.219 1.00 20.00 6 ATOM 2098 CB LEU B 336 88.031 25.292 15.023 1.00 20.00 6 ATOM 2099 CG LEU B 336 88.051 24.581 13.663 1.00 20.00 6 ATOM 2100 CD1 LEU B 336 87.486 23.177 13.787 1.00 20.00 6 ATOM 2101 CD2 LEU B 336 87.239 25.399 12.653 1.00 20.00 6 ATOM 2102 C LEU B 336 90.060 24.068 15.839 1.00 20.00 6 ATOM 2103 O LEU B 336 90.274 22.870 15.665 1.00 20.00 8 ATOM 2104 N LYS B 337 91.011 24.986 15.717 1.00 20.00 7 ATOM 2105 CA LYS B 337 92.370 24.597 15.360 1.00 20.00 6 ATOM 2106 CB LYS B 337 93.198 25.848 15.046 1.00 20.00 6 ATOM 2107 CG LYS B 337 92.678 26.560 13.801 1.00 20.00 6 ATOM 2108 CD LYS B 337 93.111 28.014 13.717 1.00 20.00 6 ATOM 2109 CE LYS B 337 94.561 28.167 13.314 1.00 20.00 6 ATOM 2110 NZ LYS B 337 94.882 29.611 13.122 1.00 20.00 7 ATOM 2111 C LYS B 337 93.020 23.764 16.467 1.00 20.00 6 ATOM 2112 O LYS B 337 93.965 23.015 16.215 1.00 20.00 8 ATOM 2113 N ALA B 338 92.495 23.866 17.684 1.00 20.00 7 ATOM 2114 CA ALA B 338 93.056 23.105 18.799 1.00 20.00 6 ATOM 2115 CB ALA B 338 92.873 23.877 20.105 1.00 20.00 6 ATOM 2116 C ALA B 338 92.441 21.718 18.929 1.00 20.00 6 ATOM 2117 O ALA B 338 92.805 20.955 19.820 1.00 20.00 8 ATOM 2118 N HIS B 339 91.513 21.375 18.043 1.00 20.00 7 ATOM 2119 CA HIS B 339 90.886 20.061 18.129 1.00 20.00 6 ATOM 2120 CB HIS B 339 89.786 19.919 17.074 1.00 20.00 6 ATOM 2121 CG HIS B 339 88.999 18.654 17.199 1.00 20.00 6 ATOM 2122 CD2 HIS B 339 87.797 18.406 17.774 1.00 20.00 6 ATOM 2123 ND1 HIS B 339 89.462 17.440 16.737 1.00 20.00 7 ATOM 2124 CE1 HIS B 339 88.578 16.498 17.021 1.00 20.00 6 ATOM 2125 NE2 HIS B 339 87.559 17.057 17.650 1.00 20.00 7 ATOM 2126 C HIS B 339 91.928 18.952 17.970 1.00 20.00 6 ATOM 2127 O HIS B 339 92.863 19.077 17.186 1.00 20.00 8 ATOM 2128 N PRO B 340 91.780 17.854 18.731 1.00 20.00 7 ATOM 2129 CD PRO B 340 90.747 17.655 19.765 1.00 20.00 6 ATOM 2130 CA PRO B 340 92.700 16.711 18.694 1.00 20.00 6 ATOM 2131 CB PRO B 340 91.966 15.665 19.521 1.00 20.00 6 ATOM 2132 CG PRO B 340 91.310 16.505 20.579 1.00 20.00 6 ATOM 2133 C PRO B 340 93.072 16.198 17.301 1.00 20.00 6 ATOM 2134 O PRO B 340 94.193 15.748 17.080 1.00 20.00 8 ATOM 2135 N PHE B 341 92.139 16.270 16.362 1.00 20.00 7 ATOM 2136 CA PHE B 341 92.407 15.797 15.011 1.00 20.00 6 ATOM 2137 CB PHE B 341 91.152 15.943 14.142 1.00 20.00 6 ATOM 2138 CG PHE B 341 91.317 15.424 12.738 1.00 20.00 6 ATOM 2139 CD1 PHE B 341 91.596 14.080 12.507 1.00 20.00 6 ATOM 2140 CD2 PHE B 341 91.182 16.277 11.647 1.00 20.00 6 ATOM 2141 CE1 PHE B 341 91.738 13.592 11.207 1.00 20.00 6 ATOM 2142 CE2 PHE B 341 91.320 15.803 10.345 1.00 20.00 6 ATOM 2143 CZ PHE B 341 91.599 14.457 10.123 1.00 20.00 6 ATOM 2144 C PHE B 341 93.571 16.550 14.362 1.00 20.00 6 ATOM 2145 O PHE B 341 94.268 16.002 13.514 1.00 20.00 8 ATOM 2146 N PHE B 342 93.777 17.800 14.765 1.00 20.00 7 ATOM 2147 CA PHE B 342 94.842 18.630 14.202 1.00 20.00 6 ATOM 2148 CB PHE B 342 94.336 20.058 13.975 1.00 20.00 6 ATOM 2149 CG PHE B 342 93.124 20.152 13.096 1.00 20.00 6 ATOM 2150 CD1 PHE B 342 93.166 19.729 11.777 1.00 20.00 6 ATOM 2151 CD2 PHE B 342 91.954 20.734 13.575 1.00 20.00 6 ATOM 2152 CE1 PHE B 342 92.058 19.888 10.936 1.00 20.00 6 ATOM 2153 CE2 PHE B 342 90.843 20.898 12.742 1.00 20.00 6 ATOM 2154 CZ PHE B 342 90.898 20.475 11.423 1.00 20.00 6 ATOM 2155 C PHE B 342 96.077 18.718 15.101 1.00 20.00 6 ATOM 2156 O PHE B 342 96.932 19.584 14.902 1.00 20.00 8 ATOM 2157 N GLU B 343 96.173 17.829 16.083 1.00 20.00 7 ATOM 2158 CA GLU B 343 97.293 17.857 17.022 1.00 20.00 6 ATOM 2159 CB GLU B 343 97.330 16.564 17.841 1.00 20.00 6 ATOM 2160 CG GLU B 343 98.475 16.525 18.839 1.00 20.00 6 ATOM 2161 CD GLU B 343 98.372 15.365 19.813 1.00 20.00 6 ATOM 2162 OE1 GLU B 343 98.290 14.201 19.359 1.00 20.00 8 ATOM 2163 OE2 GLU B 343 98.379 15.622 21.036 1.00 20.00 8 ATOM 2164 C GLU B 343 98.683 18.113 16.430 1.00 20.00 6 ATOM 2165 O GLU B 343 99.419 18.969 16.925 1.00 20.00 8 ATOM 2166 N SER B 344 99.047 17.382 15.383 1.00 20.00 7 ATOM 2167 CA SER B 344 100.370 17.549 14.781 1.00 20.00 6 ATOM 2168 CB SER B 344 100.848 16.219 14.192 1.00 20.00 6 ATOM 2169 OG SER B 344 100.072 15.856 13.065 1.00 20.00 8 ATOM 2170 C SER B 344 100.467 18.629 13.702 1.00 20.00 6 ATOM 2171 O SER B 344 101.485 18.732 13.025 1.00 20.00 8 ATOM 2172 N VAL B 345 99.423 19.435 13.544 1.00 20.00 7 ATOM 2173 CA VAL B 345 99.430 20.486 12.527 1.00 20.00 6 ATOM 2174 CB VAL B 345 97.985 20.843 12.075 1.00 20.00 6 ATOM 2175 CG1 VAL B 345 98.015 22.042 11.120 1.00 20.00 6 ATOM 2176 CG2 VAL B 345 97.335 19.646 11.400 1.00 20.00 6 ATOM 2177 C VAL B 345 100.096 21.785 12.980 1.00 20.00 6 ATOM 2178 O VAL B 345 99.844 22.275 14.085 1.00 20.00 8 ATOM 2179 N THR B 346 100.951 22.335 12.122 1.00 20.00 7 ATOM 2180 CA THR B 346 101.602 23.610 12.397 1.00 20.00 6 ATOM 2181 CB THR B 346 103.096 23.593 11.982 1.00 20.00 6 ATOM 2182 OG1 THR B 346 103.816 22.688 12.831 1.00 20.00 8 ATOM 2183 CG2 THR B 346 103.707 24.983 12.115 1.00 20.00 6 ATOM 2184 C THR B 346 100.810 24.573 11.510 1.00 20.00 6 ATOM 2185 O THR B 346 100.950 24.565 10.285 1.00 20.00 8 ATOM 2186 N TRP B 347 99.966 25.385 12.138 1.00 20.00 7 ATOM 2187 CA TRP B 347 99.089 26.306 11.425 1.00 20.00 6 ATOM 2188 CB TRP B 347 97.941 26.727 12.344 1.00 20.00 6 ATOM 2189 CG TRP B 347 97.088 25.594 12.818 1.00 20.00 6 ATOM 2190 CD2 TRP B 347 95.924 25.071 12.165 1.00 20.00 6 ATOM 2191 CE2 TRP B 347 95.436 24.008 12.963 1.00 20.00 6 ATOM 2192 CE3 TRP B 347 95.247 25.397 10.983 1.00 20.00 6 ATOM 2193 CD1 TRP B 347 97.259 24.848 13.953 1.00 20.00 6 ATOM 2194 NE1 TRP B 347 96.269 23.893 14.048 1.00 20.00 7 ATOM 2195 CZ2 TRP B 347 94.300 23.270 12.616 1.00 20.00 6 ATOM 2196 CZ3 TRP B 347 94.113 24.661 10.636 1.00 20.00 6 ATOM 2197 CH2 TRP B 347 93.654 23.610 11.452 1.00 20.00 6 ATOM 2198 C TRP B 347 99.679 27.563 10.800 1.00 20.00 6 ATOM 2199 O TRP B 347 99.101 28.114 9.867 1.00 20.00 8 ATOM 2200 N ALA B 348 100.820 28.016 11.308 1.00 20.00 7 ATOM 2201 CA ALA B 348 101.439 29.247 10.822 1.00 20.00 6 ATOM 2202 CB ALA B 348 102.582 29.656 11.761 1.00 20.00 6 ATOM 2203 C ALA B 348 101.933 29.277 9.381 1.00 20.00 6 ATOM 2204 O ALA B 348 101.874 30.323 8.738 1.00 20.00 8 ATOM 2205 N ASN B 349 102.411 28.152 8.860 1.00 20.00 7 ATOM 2206 CA ASN B 349 102.940 28.153 7.500 1.00 20.00 6 ATOM 2207 CB ASN B 349 104.466 28.205 7.569 1.00 20.00 6 ATOM 2208 CG ASN B 349 105.058 26.929 8.138 1.00 20.00 6 ATOM 2209 OD1 ASN B 349 104.445 26.282 8.984 1.00 20.00 8 ATOM 2210 ND2 ASN B 349 106.251 26.563 7.678 1.00 20.00 7 ATOM 2211 C ASN B 349 102.522 26.966 6.634 1.00 20.00 6 ATOM 2212 O ASN B 349 103.353 26.371 5.944 1.00 20.00 8 ATOM 2213 N LEU B 350 101.242 26.628 6.643 1.00 20.00 7 ATOM 2214 CA LEU B 350 100.776 25.500 5.846 1.00 20.00 6 ATOM 2215 CB LEU B 350 99.257 25.355 5.973 1.00 20.00 6 ATOM 2216 CG LEU B 350 98.734 24.848 7.316 1.00 20.00 6 ATOM 2217 CD1 LEU B 350 97.244 25.127 7.418 1.00 20.00 6 ATOM 2218 CD2 LEU B 350 99.030 23.357 7.444 1.00 20.00 6 ATOM 2219 C LEU B 350 101.147 25.574 4.365 1.00 20.00 6 ATOM 2220 O LEU B 350 101.557 24.575 3.775 1.00 20.00 8 ATOM 2221 N HIS B 351 101.006 26.744 3.752 1.00 20.00 7 ATOM 2222 CA HIS B 351 101.305 26.829 2.329 1.00 20.00 6 ATOM 2223 CB HIS B 351 100.651 28.087 1.721 1.00 20.00 6 ATOM 2224 CG HIS B 351 101.553 29.274 1.618 1.00 20.00 6 ATOM 2225 CD2 HIS B 351 102.001 30.143 2.556 1.00 20.00 6 ATOM 2226 ND1 HIS B 351 102.072 29.706 0.416 1.00 20.00 7 ATOM 2227 CE1 HIS B 351 102.798 30.792 0.618 1.00 20.00 6 ATOM 2228 NE2 HIS B 351 102.772 31.079 1.907 1.00 20.00 7 ATOM 2229 C HIS B 351 102.797 26.731 1.999 1.00 20.00 6 ATOM 2230 O HIS B 351 103.176 26.669 0.832 1.00 20.00 8 ATOM 2231 N GLN B 352 103.634 26.685 3.033 1.00 20.00 7 ATOM 2232 CA GLN B 352 105.081 26.554 2.851 1.00 20.00 6 ATOM 2233 CB GLN B 352 105.841 27.458 3.819 1.00 20.00 6 ATOM 2234 CG GLN B 352 106.395 28.705 3.166 1.00 20.00 6 ATOM 2235 CD GLN B 352 105.930 29.966 3.854 1.00 20.00 6 ATOM 2236 OE1 GLN B 352 106.134 30.139 5.053 1.00 20.00 8 ATOM 2237 NE2 GLN B 352 105.299 30.854 3.096 1.00 20.00 7 ATOM 2238 C GLN B 352 105.478 25.099 3.088 1.00 20.00 6 ATOM 2239 O GLN B 352 106.632 24.715 2.895 1.00 20.00 8 ATOM 2240 N GLN B 353 104.514 24.295 3.522 1.00 20.00 7 ATOM 2241 CA GLN B 353 104.761 22.888 3.777 1.00 20.00 6 ATOM 2242 CB GLN B 353 103.849 22.395 4.900 1.00 20.00 6 ATOM 2243 CG GLN B 353 104.122 23.050 6.240 1.00 20.00 6 ATOM 2244 CD GLN B 353 103.075 22.711 7.281 1.00 20.00 6 ATOM 2245 OE1 GLN B 353 102.627 21.571 7.377 1.00 20.00 8 ATOM 2246 NE2 GLN B 353 102.690 23.700 8.076 1.00 20.00 7 ATOM 2247 C GLN B 353 104.507 22.079 2.510 1.00 20.00 6 ATOM 2248 O GLN B 353 103.732 22.490 1.641 1.00 20.00 8 ATOM 2249 N THR B 354 105.172 20.937 2.401 1.00 20.00 7 ATOM 2250 CA THR B 354 104.998 20.071 1.244 1.00 20.00 6 ATOM 2251 CB THR B 354 106.240 19.173 1.029 1.00 20.00 6 ATOM 2252 OG1 THR B 354 107.390 19.999 0.790 1.00 20.00 8 ATOM 2253 CG2 THR B 354 106.033 18.243 −0.166 1.00 20.00 6 ATOM 2254 C THR B 354 103.777 19.197 1.501 1.00 20.00 6 ATOM 2255 O THR B 354 103.745 18.426 2.454 1.00 20.00 8 ATOM 2256 N PRO B 355 102.741 19.319 0.658 1.00 20.00 7 ATOM 2257 CD PRO B 355 102.547 20.275 −0.444 1.00 20.00 6 ATOM 2258 CA PRO B 355 101.540 18.505 0.859 1.00 20.00 6 ATOM 2259 CB PRO B 355 100.616 18.967 −0.266 1.00 20.00 6 ATOM 2260 CG PRO B 355 101.039 20.387 −0.490 1.00 20.00 6 ATOM 2261 C PRO B 355 101.835 17.011 0.766 1.00 20.00 6 ATOM 2262 O PRO B 355 102.631 16.577 −0.065 1.00 20.00 8 ATOM 2263 N PRO B 356 101.198 16.204 1.625 1.00 20.00 7 ATOM 2264 CD PRO B 356 100.128 16.522 2.587 1.00 20.00 6 ATOM 2265 CA PRO B 356 101.438 14.761 1.573 1.00 20.00 6 ATOM 2266 CB PRO B 356 100.593 14.235 2.729 1.00 20.00 6 ATOM 2267 CG PRO B 356 99.429 15.188 2.737 1.00 20.00 6 ATOM 2268 C PRO B 356 100.960 14.244 0.222 1.00 20.00 6 ATOM 2269 O PRO B 356 100.005 14.779 −0.346 1.00 20.00 8 ATOM 2270 N ALA B 357 101.629 13.221 −0.300 1.00 20.00 7 ATOM 2271 CA ALA B 357 101.247 12.660 −1.588 1.00 20.00 6 ATOM 2272 CB ALA B 357 102.352 11.750 −2.118 1.00 20.00 6 ATOM 2273 C ALA B 357 99.948 11.883 −1.427 1.00 20.00 6 ATOM 2274 O ALA B 357 99.808 11.074 −0.506 1.00 20.00 8 ATOM 2275 N LEU B 358 99.000 12.134 −2.323 1.00 20.00 7 ATOM 2276 CA LEU B 358 97.709 11.460 −2.278 1.00 20.00 6 ATOM 2277 CB LEU B 358 96.729 12.166 −3.217 1.00 20.00 6 ATOM 2278 CG LEU B 358 96.368 13.582 −2.766 1.00 20.00 6 ATOM 2279 CD1 LEU B 358 95.513 14.262 −3.813 1.00 20.00 6 ATOM 2280 CD2 LEU B 358 95.636 13.516 −1.430 1.00 20.00 6 ATOM 2281 C LEU B 358 97.813 9.976 −2.633 1.00 20.00 6 ATOM 2282 O LEU B 358 97.918 9.614 −3.806 1.00 20.00 8 ATOM 2283 N THR B 359 97.776 9.134 −1.600 1.00 20.00 7 ATOM 2284 CA THR B 359 97.867 7.678 −1.735 1.00 20.00 6 ATOM 2285 CB THR B 359 96.513 7.046 −2.149 1.00 20.00 6 ATOM 2286 OG1 THR B 359 96.111 7.555 −3.427 1.00 20.00 8 ATOM 2287 CG2 THR B 359 95.439 7.355 −1.112 1.00 20.00 6 ATOM 2288 C THR B 359 98.933 7.238 −2.736 1.00 20.00 6 ATOM 2289 O THR B 359 99.903 7.998 −2.945 1.00 20.00 8 ATOM 2290 OXT THR B 359 98.802 6.121 −3.280 1.00 20.00 8 TER ATOM 2291 OH2 TIP S 1 42.566 19.118 34.302 1.00 15.09 S ATOM 2292 OH2 TIP S 2 41.052 32.378 19.857 1.00 15.82 S ATOM 2293 OH2 TIP S 3 37.014 33.030 17.747 1.00 16.95 S ATOM 2294 OH2 TIP S 5 45.353 24.370 18.152 1.00 16.85 S ATOM 2295 OH2 TIP S 6 31.896 13.930 33.235 1.00 20.42 S ATOM 2296 OH2 TIP S 7 50.351 22.781 28.249 1.00 21.14 S ATOM 2297 OH2 TIP S 8 45.246 −0.589 −0.734 1.00 17.74 S ATOM 2298 OH2 TIP S 11 46.249 −0.348 −8.523 1.00 21.32 S ATOM 2299 OH2 TIP S 14 45.756 11.148 29.680 1.00 21.94 S ATOM 2300 OH2 TIP S 15 44.273 13.157 34.592 1.00 15.61 S ATOM 2301 OH2 TIP S 17 53.598 3.722 −1.720 1.00 21.45 S ATOM 2302 OH2 TIP S 18 46.049 13.087 31.565 1.00 20.35 S ATOM 2303 OH2 TIP S 19 53.422 22.401 −3.280 1.00 23.26 S ATOM 2304 OH2 TIP S 20 34.587 7.922 5.383 1.00 22.58 S ATOM 2305 OH2 TIP S 21 45.053 27.379 19.376 1.00 29.60 S ATOM 2306 OH2 TIP S 23 28.899 36.416 28.633 1.00 31.68 S ATOM 2307 OH2 TIP S 24 35.531 11.645 −8.219 1.00 23.45 S ATOM 2308 OH2 TIP S 25 47.364 28.787 19.612 1.00 23.03 S ATOM 2309 OH2 TIP S 27 48.859 21.588 12.634 1.00 23.76 S ATOM 2310 OH2 TIP S 29 48.805 8.920 23.626 1.00 22.23 S ATOM 2311 OH2 TIP S 31 48.619 7.247 10.112 1.00 21.32 S ATOM 2312 OH2 TIP S 34 44.824 28.720 15.621 1.00 25.27 S ATOM 2313 OH2 TIP S 35 26.030 12.634 13.407 1.00 21.61 S ATOM 2314 OH2 TIP S 36 50.462 19.810 40.066 1.00 25.45 S ATOM 2315 OH2 TIP S 37 39.631 23.510 −0.239 1.00 30.88 S ATOM 2316 OH2 TIP S 40 44.734 42.655 10.346 1.00 30.84 S ATOM 2317 OH2 TIP S 41 54.653 3.902 1.503 1.00 27.14 S ATOM 2318 OH2 TIP S 45 45.693 21.923 39.754 1.00 28.30 S ATOM 2319 OH2 TIP S 47 47.820 16.413 7.805 1.00 25.73 S ATOM 2320 OH2 TIP S 48 50.292 31.412 29.642 1.00 32.79 S ATOM 2321 OH2 TIP S 49 26.056 16.646 34.827 1.00 29.80 S ATOM 2322 OH2 TIP S 52 31.714 10.996 31.855 1.00 29.15 S ATOM 2323 OH2 TIP S 53 46.108 23.843 −4.299 1.00 24.21 S ATOM 2324 OH2 TIP S 54 37.645 11.206 34.448 1.00 28.56 S ATOM 2325 OH2 TIP S 55 26.371 28.513 12.142 1.00 32.08 S ATOM 2326 OH2 TIP S 58 33.564 19.700 3.483 1.00 28.28 S ATOM 2327 OH2 TIP S 64 48.295 −0.632 14.280 1.00 32.13 S ATOM 2328 OH2 TIP S 65 40.064 26.036 34.324 1.00 24.17 S ATOM 2329 OH2 TIP S 66 29.570 3.958 14.729 1.00 28.94 S ATOM 2330 OH2 TIP S 72 60.085 11.604 6.814 1.00 38.35 S ATOM 2331 OH2 TIP S 73 39.203 44.403 18.686 1.00 26.61 S ATOM 2332 OH2 TIP S 76 47.312 12.366 27.366 1.00 28.51 S ATOM 2333 OH2 TIP S 80 43.862 33.771 33.329 1.00 28.82 S ATOM 2334 OH2 TIP S 81 57.890 13.106 2.128 1.00 40.62 S ATOM 2335 OH2 TIP S 82 41.663 34.381 32.043 1.00 19.35 S ATOM 2336 OH2 TIP S 85 50.974 40.331 19.200 1.00 21.14 S ATOM 2337 OH2 TIP S 88 47.925 −0.832 −6.556 1.00 24.11 S ATOM 2338 OH2 TIP S 90 27.231 28.336 33.481 1.00 27.64 S ATOM 2339 OH2 TIP S 91 43.651 −7.101 −7.995 1.00 24.33 S ATOM 2340 OH2 TIP S 92 49.325 4.387 19.370 1.00 28.02 S ATOM 2341 OH2 TIP S 93 46.231 11.549 33.898 1.00 29.40 S ATOM 2342 OH2 TIP S 94 63.889 24.831 1.168 1.00 26.53 S ATOM 2343 OH2 TIP S 96 56.396 4.952 −6.749 1.00 28.00 S ATOM 2344 OH2 TIP S 98 35.510 27.986 11.558 1.00 29.24 S ATOM 2345 OH2 TIP S 100 49.942 24.366 30.265 1.00 31.61 S ATOM 2346 OH2 TIP S 101 56.121 7.113 −8.298 1.00 31.57 S ATOM 2347 OH2 TIP S 102 58.318 19.957 −8.378 1.00 26.95 S ATOM 2348 OH2 TIP S 103 49.647 22.446 39.624 1.00 40.57 S ATOM 2349 OH2 TIP S 104 45.359 7.052 13.052 1.00 26.27 S ATOM 2350 OH2 TIP S 105 37.150 32.340 32.346 1.00 34.45 S ATOM 2351 OH2 TIP S 107 43.465 40.457 8.240 1.00 40.48 S ATOM 2352 OH2 TIP S 119 36.644 8.257 13.418 1.00 30.70 S ATOM 2353 OH2 TIP S 123 41.912 −8.974 −8.264 1.00 26.08 S ATOM 2354 OH2 TIP S 124 62.424 15.800 −7.411 1.00 24.08 S ATOM 2355 OH2 TIP S 126 37.266 18.656 −9.097 1.00 28.99 S ATOM 2356 OH2 TIP S 127 43.129 26.845 14.606 1.00 25.19 S ATOM 2357 OH2 TIP S 128 36.339 32.639 29.802 1.00 29.25 S ATOM 2358 OH2 TIP S 130 54.051 14.561 26.498 1.00 33.93 S ATOM 2359 OH2 TIP S 131 41.805 −4.242 5.492 1.00 33.72 S ATOM 2360 OH2 TIP S 133 38.873 25.163 36.697 1.00 30.69 S ATOM 2361 OH2 TIP S 134 28.777 8.553 25.307 1.00 31.43 S ATOM 2362 OH2 TIP S 135 53.672 10.546 −12.803 1.00 33.45 S ATOM 2363 OH2 TIP S 136 59.892 15.434 11.467 1.00 31.39 S ATOM 2364 OH2 TIP S 137 31.040 12.361 35.470 1.00 34.07 S ATOM 2365 OH2 TIP S 139 33.489 14.292 −0.598 1.00 40.68 S ATOM 2366 OH2 TIP S 140 46.918 8.748 11.662 1.00 29.23 S ATOM 2367 OH2 TIP S 141 46.297 −7.287 −9.196 1.00 42.20 S ATOM 2368 OH2 TIP S 142 58.193 6.715 −4.685 1.00 35.48 S ATOM 2369 OH2 TIP S 143 44.598 4.435 12.503 1.00 27.68 S ATOM 2370 OH2 TIP S 144 27.003 5.999 12.450 1.00 36.30 S ATOM 2371 OH2 TIP S 145 43.676 32.852 35.735 1.00 35.70 S ATOM 2372 OH2 TIP S 146 35.783 18.628 36.452 1.00 34.62 S ATOM 2373 OH2 TIP S 147 25.402 4.058 20.638 1.00 45.03 S ATOM 2374 OH2 TIP S 148 45.839 35.853 33.724 1.00 35.47 S ATOM 2375 OH2 TIP S 149 22.176 18.976 16.752 1.00 31.87 S ATOM 2376 OH2 TIP S 150 43.986 33.179 10.162 1.00 37.70 S ATOM 2377 OH2 TIP S 151 50.653 20.347 42.428 1.00 35.80 S ATOM 2378 OH2 TIP S 152 47.843 24.314 9.506 1.00 31.05 S ATOM 2379 OH2 TIP S 153 44.693 5.273 −14.175 1.00 29.90 S ATOM 2380 OH2 TIP S 155 26.560 36.851 31.684 1.00 49.29 S ATOM 2381 OH2 TIP S 156 46.867 8.019 −12.951 1.00 29.21 S ATOM 2382 OH2 TIP S 157 30.432 28.741 12.438 1.00 37.76 S ATOM 2383 OH2 TIP S 158 41.004 20.553 6.423 1.00 39.53 S ATOM 2384 OH2 TIP S 159 49.258 20.069 29.294 1.00 33.97 S ATOM 2385 OH2 TIP S 160 48.082 28.459 16.489 1.00 33.10 S ATOM 2386 OH2 TIP S 161 47.448 18.625 27.683 1.00 34.87 S ATOM 2387 OH2 TIP S 162 19.687 20.632 23.411 1.00 35.01 S ATOM 2388 OH2 TIP S 163 32.402 −1.266 22.443 1.00 37.26 S ATOM 2389 OH2 TIP S 164 39.475 33.468 33.237 1.00 35.34 S ATOM 2390 OH2 TIP S 165 44.277 18.950 5.162 1.00 45.14 S ATOM 2391 OH2 TIP S 166 34.797 30.523 10.736 1.00 47.55 S ATOM 2392 OH2 TIP S 167 46.541 3.526 −14.949 1.00 26.54 S ATOM 2393 OH2 TIP S 168 36.333 16.371 1.539 1.00 38.68 S ATOM 2394 OH2 TIP S 169 46.761 38.936 27.403 1.00 34.66 S ATOM 2395 OH2 TIP S 170 24.163 13.264 11.375 1.00 41.23 S ATOM 2396 OH2 TIP S 171 48.459 15.018 31.951 1.00 38.11 S ATOM 2397 OH2 TIP S 172 34.261 23.193 40.004 1.00 48.96 S ATOM 2398 OH2 TIP S 173 45.924 −0.026 13.224 1.00 39.55 S ATOM 2399 OH2 TIP S 175 41.384 37.389 32.543 1.00 40.74 S ATOM 2400 OH2 TIP S 177 49.394 35.312 27.150 1.00 44.33 S ATOM 2401 OH2 TIP S 178 29.066 29.942 34.359 1.00 41.46 S ATOM 2402 OH2 TIP S 180 49.354 19.467 7.273 1.00 34.56 S ATOM 2403 OH2 TIP S 181 25.298 17.029 31.863 1.00 47.74 S ATOM 2404 OH2 TIP S 182 37.071 25.027 4.669 1.00 43.87 S ATOM 2405 OH2 TIP S 183 22.581 7.487 18.691 1.00 41.75 S ATOM 2406 OH2 TIP S 184 32.269 7.011 −1.891 1.00 48.84 S ATOM 2407 OH2 TIP S 185 48.234 0.494 6.833 1.00 48.16 S ATOM 2408 OH2 TIP S 187 20.008 14.658 19.211 1.00 45.27 S ATOM 2409 OH2 TIP S 188 49.341 22.698 42.272 1.00 42.20 S ATOM 2410 OH2 TIP S 190 61.292 18.260 −8.097 1.00 45.21 S ATOM 2411 OH2 TIP S 191 28.152 10.606 2.819 1.00 40.38 S ATOM 2412 OH2 TIP S 192 25.626 12.619 23.191 1.00 34.27 S ATOM 2413 OH2 TIP S 193 59.876 11.603 1.216 1.00 46.54 S ATOM 2414 OH2 TIP S 194 57.592 21.183 −10.646 1.00 45.82 S ATOM 2415 OH2 TIP S 195 31.509 36.649 21.499 1.00 38.73 S ATOM 2416 OH2 TIP S 197 50.270 −1.543 −6.136 1.00 42.66 S ATOM 2417 OH2 TIP S 198 24.467 8.729 13.088 1.00 42.78 S ATOM 2418 OH2 TIP S 199 38.098 8.699 25.759 1.00 32.80 S ATOM 2419 OH2 TIP S 200 57.831 11.358 −13.255 1.00 45.31 S ATOM 2420 OH2 TIP S 201 23.888 22.328 30.524 1.00 37.12 S ATOM 2421 OH2 TIP S 202 47.691 26.068 37.666 1.00 37.92 S ATOM 2422 OH2 TIP S 203 38.653 7.070 29.307 1.00 50.54 S ATOM 2423 OH2 TIP S 206 44.424 27.583 2.092 1.00 53.50 S ATOM 2424 OH2 TIP S 212 22.258 2.296 17.948 1.00 47.38 S ATOM 2425 OH2 TIP S 214 19.843 17.943 23.303 1.00 30.36 S ATOM 2426 OH2 TIP S 216 27.647 11.344 24.681 1.00 31.32 S ATOM 2427 OH2 TIP S 217 37.953 7.817 −9.284 1.00 45.97 S ATOM 2428 OH2 TIP S 218 33.845 34.040 12.124 1.00 38.11 S ATOM 2429 OH2 TIP S 219 58.484 15.269 13.717 1.00 38.26 S ATOM 2430 OH2 TIP S 220 48.526 40.920 26.583 1.00 35.23 S ATOM 2431 OH2 TIP S 222 52.094 21.184 38.122 1.00 29.86 S ATOM 2432 OH2 TIP S 223 36.889 5.881 3.281 1.00 37.63 S ATOM 2433 OH2 TIP S 224 47.642 −1.401 −10.684 1.00 34.89 S ATOM 2434 OH2 TIP S 226 47.284 2.916 19.133 1.00 34.10 S ATOM 2435 OH2 TIP S 227 42.468 4.463 −15.039 1.00 37.98 S ATOM 2436 OH2 TIP S 228 19.169 22.832 21.831 1.00 41.57 S ATOM 2437 OH2 TIP S 231 57.592 12.689 14.880 1.00 50.22 S ATOM 2438 OH2 TIP S 232 27.102 9.176 5.655 1.00 40.57 S ATOM 2439 OH2 TIP S 233 58.618 9.072 −11.925 1.00 50.71 S ATOM 2440 OH2 TIP S 234 22.822 25.342 19.945 1.00 34.93 S ATOM 2441 OH2 TIP S 236 24.831 32.218 28.901 1.00 37.69 S ATOM 2442 OH2 TIP S 237 20.045 10.774 16.992 1.00 39.57 S ATOM 2443 OH2 TIP S 238 58.019 19.850 15.679 1.00 41.42 S ATOM 2444 OH2 TIP S 239 19.490 20.949 26.114 1.00 34.55 S ATOM 2445 OH2 TIP S 240 61.187 26.377 7.346 1.00 39.68 S ATOM 2446 OH2 TIP S 241 33.680 38.342 19.389 1.00 48.93 S ATOM 2447 OH2 TIP S 242 51.539 31.612 10.881 1.00 55.65 S ATOM 2448 OH2 TIP S 244 25.872 14.431 30.404 1.00 46.69 S ATOM 2449 OH2 TIP S 248 37.332 5.849 9.544 1.00 43.81 S ATOM 2450 OH2 TIP S 250 39.087 −1.293 −9.655 1.00 42.96 S ATOM 2451 OH2 TIP S 258 23.938 30.000 30.010 1.00 38.89 S ATOM 2452 OH2 TIP S 259 24.949 29.749 32.578 1.00 40.17 S ATOM 2453 OH2 TIP S 260 32.111 17.986 1.918 1.00 48.36 S ATOM 2454 OH2 TIP S 266 21.404 12.876 25.603 1.00 57.17 S ATOM 2455 OH2 TIP S 269 35.425 36.767 12.550 1.00 30.70 S ATOM 2456 OH2 TIP S 270 52.438 25.529 30.131 1.00 44.85 S ATOM 2457 OH2 TIP S 271 53.299 20.156 36.003 1.00 37.15 S ATOM 2458 OH2 TIP S 272 50.914 6.919 23.723 1.00 43.29 S ATOM 2459 OH2 TIP S 274 31.578 30.795 11.014 1.00 50.15 S ATOM 2460 OH2 TIP S 275 26.341 7.243 22.447 1.00 39.40 S ATOM 2461 OH2 TIP S 276 60.392 18.195 10.235 1.00 37.91 S ATOM 2462 OH2 TIP S 277 47.355 −9.081 −10.821 1.00 48.18 S ATOM 2463 OH2 TIP S 279 41.304 6.175 −16.647 1.00 38.12 S ATOM 2464 OH2 TIP S 282 33.299 21.620 37.881 1.00 46.29 S ATOM 2465 OH2 TIP S 283 56.469 26.112 −8.575 1.00 43.71 S ATOM 2466 OH2 TIP S 287 48.382 26.573 7.246 1.00 41.43 S ATOM 2467 OH2 TIP S 288 56.240 7.245 −11.331 1.00 41.79 S ATOM 2468 OH2 TIP S 290 49.060 14.978 28.166 1.00 37.03 S ATOM 2469 OH2 TIP S 291 37.095 44.270 26.442 1.00 45.08 S ATOM 2470 OH2 TIP S 292 47.814 −0.384 −13.299 1.00 48.60 S ATOM 2471 OH2 TIP S 297 58.081 2.784 −7.841 1.00 41.89 S ATOM 2472 OH2 TIP S 298 36.447 45.321 18.644 1.00 54.91 S ATOM 2473 OH2 TIP S 299 49.029 23.328 1.767 1.00 30.55 S ATOM 2474 OH2 TIP S 301 24.375 13.771 8.634 1.00 48.47 S ATOM 2475 OH2 TIP S 303 47.904 36.798 28.653 1.00 35.76 S ATOM 2476 OH2 TIP S 305 51.156 40.821 27.172 1.00 43.59 S ATOM 2477 OH2 TIP S 306 32.943 28.917 35.227 1.00 42.60 S ATOM 2478 OH2 TIP S 307 58.462 28.373 6.251 1.00 46.15 S ATOM 2479 OH2 TIP S 308 41.964 30.940 36.712 1.00 48.26 S ATOM 2480 OH2 TIP S 313 51.176 −1.922 −3.336 1.00 50.61 S ATOM 2481 OH2 TIP S 1001 21.319 36.868 23.805 1.00 36.97 S ATOM 2482 OH2 TIP S 1002 48.880 32.620 27.617 1.00 44.40 S ATOM 2483 OH2 TIP S 1003 61.880 19.473 11.767 1.00 45.49 S ATOM 2484 OH2 TIP S 1004 52.770 21.424 26.815 1.00 24.43 S ATOM 2485 OH2 TIP S 1005 35.373 29.094 36.197 1.00 35.97 S ATOM 2486 OH2 TIP S 1006 40.815 −6.636 4.389 1.00 43.15 S ATOM 2487 OH2 TIP S 1007 44.953 1.286 11.272 1.00 49.45 S ATOM 2488 OH2 TIP S 1010 21.004 16.168 27.009 1.00 48.51 S ATOM 2489 OH2 TIP S 1011 47.094 41.786 9.243 1.00 50.10 S ATOM 2490 OH2 TIP S 1012 32.479 2.978 14.158 1.00 49.47 S ATOM 2491 O12 GLC G 1 48.557 11.372 −12.279 1.00 40.72 G ATOM 2492 C11 GLC G 1 48.836 12.133 −11.097 1.00 38.05 G ATOM 2493 C13 GLC G 1 49.266 13.554 −11.476 1.00 38.09 G ATOM 2494 O14 GLC G 1 49.559 14.299 −10.292 1.00 33.99 G ATOM 2495 C15 GLC G 1 48.150 14.257 −12.257 1.00 37.32 G ATOM 2496 O16 GLC G 1 48.574 15.582 −12.604 1.00 36.74 G ATOM 2497 O12 GLC G 2 40.114 −6.634 −6.562 1.00 33.52 G ATOM 2498 C11 GLC G 2 38.967 −6.592 −7.404 1.00 31.05 G ATOM 2499 C13 GLC G 2 37.712 −6.417 −6.552 1.00 31.56 G ATOM 2500 O14 GLC G 2 36.554 −6.406 −7.389 1.00 30.70 G ATOM 2501 C15 GLC G 2 37.792 −5.109 −5.761 1.00 30.03 G ATOM 2502 O16 GLC G 2 36.609 −4.961 −4.975 1.00 29.66 G ATOM 2503 O12 GLC G 3 44.030 8.243 −13.470 1.00 37.90 G ATOM 2504 C11 GLC G 3 43.950 9.648 −13.690 1.00 38.47 G ATOM 2505 C13 GLC G 3 42.747 9.974 −14.579 1.00 39.52 G ATOM 2506 O14 GLC G 3 41.551 9.526 −13.942 1.00 39.39 G ATOM 2507 C15 GLC G 3 42.878 9.280 −15.934 1.00 41.43 G ATOM 2508 O16 GLC G 3 41.736 9.613 −16.731 1.00 40.78 G ATOM 2509 O12 GLC G 5 40.556 1.005 2.289 1.00 45.25 G ATOM 2510 C11 GLC G 5 40.966 2.332 1.960 1.00 40.56 G ATOM 2511 C13 GLC G 5 40.187 3.327 2.814 1.00 40.36 G ATOM 2512 O14 GLC G 5 38.791 3.169 2.572 1.00 40.71 G ATOM 2513 C15 GLC G 5 40.619 4.751 2.464 1.00 40.04 G ATOM 2514 O16 GLC G 5 39.885 5.681 3.256 1.00 36.89 G ATOM 2515 O12 GLC G 6 36.951 22.702 40.046 1.00 63.04 G ATOM 2516 C11 GLC G 6 37.592 21.583 39.422 1.00 62.46 G ATOM 2517 C13 GLC G 6 38.104 21.978 38.030 1.00 61.14 G ATOM 2518 O14 GLC G 6 39.034 23.054 38.168 1.00 61.72 G ATOM 2519 C15 GLC G 6 36.948 22.429 37.126 1.00 60.51 G ATOM 2520 O16 GLC G 6 35.992 21.372 36.960 1.00 58.61 G ATOM 2521 O12 GLC G 7 37.316 0.281 14.299 1.00 73.45 G ATOM 2522 C11 GLC G 7 37.655 −0.758 15.222 1.00 72.78 G ATOM 2523 C13 GLC G 7 36.592 −1.856 15.157 1.00 72.98 G ATOM 2524 O14 GLC G 7 35.320 −1.299 15.498 1.00 73.88 G ATOM 2525 C15 GLC G 7 36.924 −2.989 16.134 1.00 73.66 G ATOM 2526 O16 GLC G 7 36.972 −2.493 17.478 1.00 75.38 G ATOM 2527 O12 GLC G 8 51.921 21.898 5.908 1.00 62.51 G ATOM 2528 C11 GLC G 8 52.447 20.871 5.063 1.00 63.42 G ATOM 2529 C13 GLC G 8 51.476 20.597 3.908 1.00 64.28 G ATOM 2530 O14 GLC G 8 51.297 21.794 3.150 1.00 66.28 G ATOM 2531 C15 GLC G 8 50.121 20.137 4.448 1.00 64.49 G ATOM 2532 O16 GLC G 8 49.233 19.886 3.357 1.00 64.01 G ATOM 2533 O12 GLC G 10 36.044 37.499 29.523 1.00 56.89 G ATOM 2534 C11 GLC G 10 35.164 36.645 30.259 1.00 56.97 G ATOM 2535 C13 GLC G 10 33.849 36.489 29.494 1.00 56.11 G ATOM 2536 O14 GLC G 10 33.248 37.772 29.308 1.00 56.44 G ATOM 2537 C15 GLC G 10 32.900 35.580 30.277 1.00 55.84 G ATOM 2538 O16 GLC G 10 31.674 35.442 29.557 1.00 55.39 G ATOM 2539 O3G ATP N 1 46.280 25.658 5.170 1.00 51.49 N ATOM 2540 PG ATP N 1 46.464 25.053 3.691 1.00 52.22 N ATOM 2541 O1G ATP N 1 47.406 23.911 3.763 1.00 51.41 N ATOM 2542 O2G ATP N 1 46.794 26.182 2.784 1.00 52.07 N ATOM 2543 O3B ATP N 1 44.976 24.513 3.344 1.00 51.01 N ATOM 2544 PB ATP N 1 44.560 22.969 3.605 1.00 50.20 N ATOM 2545 O1B ATP N 1 43.083 22.898 3.669 1.00 49.41 N ATOM 2546 O2B ATP N 1 45.345 22.474 4.766 1.00 50.34 N ATOM 2547 O3A ATP N 1 45.070 22.231 2.255 1.00 47.77 N ATOM 2548 PA ATP N 1 45.075 20.613 2.121 1.00 42.84 N ATOM 2549 O1A ATP N 1 45.547 20.291 0.754 1.00 43.81 N ATOM 2550 O2A ATP N 1 45.807 20.035 3.270 1.00 45.03 N ATOM 2551 O5* ATP N 1 43.516 20.223 2.245 1.00 41.73 N ATOM 2552 C5* ATP N 1 42.528 20.925 1.489 1.00 37.57 N ATOM 2553 C4* ATP N 1 41.127 20.379 1.776 1.00 39.45 N ATOM 2554 O4* ATP N 1 40.907 19.024 1.279 1.00 37.72 N ATOM 2555 C3* ATP N 1 40.777 20.321 3.251 1.00 38.48 N ATOM 2556 O3* ATP N 1 40.360 21.615 3.697 1.00 40.42 N ATOM 2557 C2* ATP N 1 39.608 19.374 3.270 1.00 37.58 N ATOM 2558 O2* ATP N 1 38.410 20.076 2.924 1.00 35.98 N ATOM 2559 C1* ATP N 1 39.939 18.346 2.173 1.00 35.55 N ATOM 2560 N9 ATP N 1 40.628 17.156 2.747 1.00 31.76 N ATOM 2561 C8 ATP N 1 41.864 17.126 3.274 1.00 30.49 N ATOM 2562 N7 ATP N 1 42.143 15.877 3.667 1.00 29.75 N ATOM 2563 C5 ATP N 1 41.088 15.118 3.390 1.00 27.49 N ATOM 2564 C4 ATP N 1 40.125 15.925 2.810 1.00 30.02 N ATOM 2565 N3 ATP N 1 38.937 15.389 2.431 1.00 27.11 N ATOM 2566 C2 ATP N 1 38.679 14.085 2.615 1.00 25.62 N ATOM 2567 N1 ATP N 1 39.597 13.283 3.175 1.00 21.76 N ATOM 2568 C6 ATP N 1 40.800 13.768 3.571 1.00 23.90 N ATOM 2569 N6 ATP N 1 41.698 12.964 4.127 1.00 21.94 N ATOM 2570 S SO4 I 1 58.680 8.493 −0.639 1.00 56.05 I ATOM 2571 O1 SO4 I 1 57.956 7.875 0.483 1.00 58.83 I ATOM 2572 O2 SO4 I 1 57.886 9.607 −1.188 1.00 57.04 I ATOM 2573 O3 SO4 I 1 58.906 7.478 −1.683 1.00 57.47 I ATOM 2574 O4 SO4 I 1 59.976 9.008 −0.156 1.00 57.51 I ATOM 2575 S SO4 I 2 39.339 4.855 7.057 1.00 84.24 I ATOM 2576 O1 SO4 I 2 39.390 6.175 7.711 1.00 85.02 I ATOM 2577 O2 SO4 I 2 40.101 4.897 5.797 1.00 84.75 I ATOM 2578 O3 SO4 I 2 37.936 4.506 6.766 1.00 84.94 I ATOM 2579 O4 SO4 I 2 39.931 3.842 7.954 1.00 84.44 I ATOM 2580 S SO4 I 3 38.987 −2.256 3.310 1.00 58.58 I ATOM 2581 O1 SO4 I 3 37.734 −1.675 3.827 1.00 59.11 I ATOM 2582 O2 SO4 I 3 39.460 −1.454 2.172 1.00 59.91 I ATOM 2583 O3 SO4 I 3 38.743 −3.640 2.866 1.00 60.97 I ATOM 2584 O4 SO4 I 3 40.014 −2.260 4.369 1.00 59.58 I ATOM 2585 S SO4 I 4 34.397 5.289 30.981 1.00 64.34 I ATOM 2586 O1 SO4 I 4 33.627 6.528 30.742 1.00 60.43 I ATOM 2587 O2 SO4 I 4 34.337 4.427 29.782 1.00 60.11 I ATOM 2588 O3 SO4 I 4 33.816 4.572 32.133 1.00 64.39 I ATOM 2589 O4 SO4 I 4 35.806 5.626 31.277 1.00 63.55 I ATOM 2590 S SO4 I 5 55.074 −6.984 −3.711 1.00 75.40 I ATOM 2591 O1 SO4 I 5 54.657 −7.518 −2.399 1.00 74.66 I ATOM 2592 O2 SO4 I 5 54.209 −5.845 −4.065 1.00 74.96 I ATOM 2593 O3 SO4 I 5 54.950 −8.034 −4.742 1.00 74.22 I ATOM 2594 O4 SO4 I 5 56.477 −6.532 −3.633 1.00 75.15 I ATOM 2595 O2 PO4 P 100 57.362 24.998 13.149 1.00 66.76 P ATOM 2596 O3 PO4 P 100 59.399 26.166 13.761 1.00 66.89 P ATOM 2597 O4 PO4 P 100 57.761 25.606 15.462 1.00 67.43 P ATOM 2598 O1 PO4 P 100 57.264 27.325 13.818 1.00 65.91 P ATOM 2599 P PO4 P 100 57.947 26.025 14.048 1.00 66.69 P END

Example 5 PDK1 Fragments

We produced constructs for expression of different forms of PDK1 in bacteria. The constructs were either in TRC vectors, pET-15b vector and pGEX expression vector to enable the expression of GST fused N-terminally to PDK1. PDK1 expressed from pGEX 51-556 (ie residues 51 to 556 of PDK1) was found to be highly degraded.

PDK1 protein was also expressed with N-terminal His tags from vector TRC comprising PDK1 sequences 51-556, 51-404 and 1-360, or pET15b 51-404 and tested for expression levels and activity. The expression was generally low, around 0.2 mg/L culture. The specific activity was lower than the His-tagged 51-556 protein purified from baculovirus cells. In the case of PDK1 51-404 expressed from pET-15b construct the level of expression turned out to be very variable. This was probably due to instability of the plasmid since we produced evidence that after a growth of 0.2 units of absorbance, (as measured in a spectrophotometer at 600 nm wavelength) the cells growing faster in the culture were actually not harbouring the plasmid with ampiciline resistance. The instability of the plasmid can be due to toxicity produced by basal expression of PDK1. Although production in bacteria was the theoretical best expression system to avoid heterogeneity due to the different extent of phosphorylation of the different phosphorylation sites in hPDK1, it was found that the protein was either degraded, expressed to low levels, had 5 times less specific activity, or was possibly toxic.

The His-tagged purified PDK1 51-556 protein obtained from baculovirus expression system was homogeneous as depicted by the appearance of one band after by SDS-PAGE analysis of a sample.

Nevertheless, the analysis after isoelectric focussing revealed a large smear of protein covering several units of pH. This analysis suggested that the protein was not homogeneous in terms of its isoelectric point, possibly due to the number of phosphorylation sites which were not homogeneously phosphorylated. This protein did not crystallise.

We purified to homogeneity a truncated His-Myc tagged PDK1 (51-404) which lacks the N-terminal 50 residues and the C-terminal 152 residues which include the PH domain. This protein, produced by a baculovirus expression system, had similar characteristics to the full length wild type PDK1 in terms of its activity towards the peptide substrate T308tide, its activation by the peptide PIFtide, and the binding to PIFtide (as analysed by BiaCore). The purified protein was screened for crystallisation conditions using Hampton Research kits (144 different conditions). Crystallisation conditions were screened with two concentrations of PDK1, in the presence or absence of PIFtide, Staurosporine, at 20° C. and in the presence of PIFtide at 4° C. No protein crystals were observed after 6 months, suggesting that this construct was not suitable for forming crystals although all other characteristics were similar to wild type protein.

The His-Myc PDK1 51-404 purified protein was also subjected to protease treatments in order to obtain a protease-insensitive molecule for increasing the chances of obtaining a shorter, stable variant of PDK1. Different protease treatments were tested. Treatment with Glu-C produced a polypeptide of approximately 38 KDa which was stable. This PDK1 protein was active and lacked the His-tag and part of the Myc-tag, and possibly part of the C-terminal residues. This protein was also set up for crystallography screenings. Some crystals were obtained using this preparation after 4 months, but they were not followed up.

A protein kinase corresponding to residues PDk1 51-387 was also produced, in an identical vector to that used to produce the protein PDK1 51-359. Interestingly, this protein was similar to wild type and PDK1 51-404, but had extreme problems for concentration using conventional methods. The protein could not be concentrated further than 2.5 mg/ml, and no crystals were obtained using this construct.

The PDK1 protein that finally crystallised is lacking the first 50 aminoacids and was constructed to end at position 359. This protein was stable in the absence of the PH domain and aminoacids that in hPDK1 link the catalytic domain with the PH domain. The construct PDK1 51-359 was also short enough that no other described phosphorylation sites besides activation loop phosphorylation site 241 were present.

Example 6 Structural Basis for UCN-01 Specificity and PDK1 Inhibition

The staurosporine derivative UCN-01 (7-hydroxyl staurosporine) has been reported to be a potent inhibitor for PDK1 and is currently in clinical trials for the treatment of cancer. Here we report the crystal structures of staurosporine and UCN-01 in complex with the kinase domain of PDK1. We show that although staurosporine and UCN-01 interact with the PDK1 active site in an overall similar manner, the UCN-0,7-hydroxyl group, which is not present on staurosporine, generates direct and water-mediated hydrogen bonds with active site residues. Inhibition data from UCN-01 tested against a panel of 29 different kinases show a different pattern of inhibition compared to staurosporine. We discuss how these differences in inhibition could be attributed to specific interactions with the additional 7-hydroxyl-group as well as by the size of the 7-hydroxyl-binding pocket. This information could lead to opportunities for structure-based optimisation of PDK1 inhibitors.

Insulin and growth factor signalling is mediated by the activation of a lipid kinase, phosphatidylinositol-3-kinase (PI3K), which produces the second messenger molecule phosphatidylinositol(3,4,5)trisphosphate (PtdIns(3,4,5)P) [1]. Upon generation of PtdIns(3,4,5)P, 3-Phosphoinositide Dependent protein Kinase-1 (PDK1) and protein kinase B (PKB, also known as Akt) are co-localised at the plasma membrane through interaction of their Pleckstrin Homology (PH) domains with PtdIns(3,4,5)P [2,3]. PDK1 activates PKB by phosphorylation of its T-loop (Thr308 in PKB) [4, 5]. PDK1 also activates other protein kinases related to PKB, including isoforms of p70 ribosomal S6 kinase (S6K) [6], serum and glucocorticoid responsive kinases (SGK) [7] and p90 ribosomal S6 kinase (Rsk) [8]. These kinases lack PH domains and do not bind PtdIns(3,4,5)P3, and are thought to be activated by a different mechanism, in which the substrates require a priming phosphorylation in a conserved hydrophobic motif (HM) at their C-terminus (reviewed in [9]). This phosphorylation creates a docking motif that specifically interacts with a pocket on the N-terminal lobe of the PDK1 kinase domain (termed PDK1 interacting fragment (PIF) pocket) [10,11] bringing PDK1 together with its substrate and enabling PDK1 to phosphorylate these kinases in their T-loop, thereby activating them. A significant number of human cancers possess elevated PtdIns(3,4,5)P levels due to mutations in a number of genes that regulate the production and degradation of this 3-phosphoinositide. One of the most frequently found mutations occurs in the PtdIns(3,4,5)P 3-phosphatase (PTEN) resulting in constitutive activation of PKB and S6K, which are thought to be major contributors to the proliferation and the survival of such tumour cells [12]. Thus, inhibitors of PDK1 have the potential to act as anti-cancer agents as they would be expected to suppress activation of S6K and PKB and inhibit cell growth and induce apoptosis of cancer cells that possess elevated levels of PtdIns(3,4,5)P.

PDK1 consists of an N-terminal kinase domain and a C-terminal PH-domain [13]. The structure of the PDK1 kinase domain has been solved (see the preceding Examples and [11]) and leads to a definition of the residues lining the ATP binding site and an understanding of the PDK1 activation mechanism. The PIFbinding pocket could be identified, together with a specific pocket for the phosphorylated Ser/Thr residue on the HM of substrate kinases. Staurosporine, a natural product ATP-competitive inhibitor, inhibits many kinases in the low nM range [14], and therefore displays a high cytotoxicity [15]. UCN-01 (7-hydroxyl staurosporine) is a derivative with an additional hydroxyl group on the lactam ring (FIG. 1). It was originally described as a PKC-selective inhibitor isolated from Streptomyces sp. cultures [16], although further studies showed it to be more non-specific [14, 17]. UCN-01 potently inhibits the growth and induces apoptosis of many cancer cells and these effects are thought to be unrelated to PKC inhibition [18, 19]. Due to its anti-tumour activity in vivo and in vitro, UCN-01 is currently undergoing clinical trials with positive effects being reported in the phase 1 studies (reviewed in [19]). Recent reports suggested the cell cycle checkpoint kinase Chk1 [20] and PDK1 [21] may be key targets of UCN-01 in inhibiting the growth of cancer cells, as both kinases are inhibited by UCN-01 in the low nM range.

Here we report the structures of the PDK1 kinase domain in complex with staurosporine and UCN-01, demonstrating the presence of a pocket that accommodates the 7-hydroxyl group of UCN-01. Specificity tests against a panel of 29 kinases shows that although both staurosporine and UCN-01 are relatively non-specific inhibitors, the fingerprint analysis of UCN-01 inhibition with a panel of protein kinases is significantly different from that of staurosporine. We also perform analysis of residues predicted to line the UCN-01 hydroxyl pocket on a number or protein kinases, and propose a general model that could account for the different sensitivity of protein kinases for staurosporine and UCN-01.

Methods

Expression, Purification and Crystallisation

Human PDK1 (residues 51-359) was expressed using a baculovirus mediated infection of the SF21 insect cell line and purified as described in the preceding examples and [11] with the following differences: After elution of the His-tagged protein from the Ni-NTA-agarose beads with 200 mM imidazole, the protein was dialysed against 250 mM NaCl, 25 mM Tris pH 7.5, 1 mM DTT for 3 hours at 4° C. Proteolysis with GST-tagged PreScission protease was performed overnight at 4° C.

For crystals of the PDK1-UCN-01 complex, 100 μl of PDK1 at a concentration of 6.6 mg/ml was mixed with 30 μl UCN-01 (5.3 mM in 50% ethanol) and incubated on ice for 2 hours. The protein was crystallized using sitting drop vapour diffusion. 1.25 μl of protein solution was mixed with 0.25 μl cobaltous chloride hexahydrate (0.1 M) and 1 μl mother liquor, consisting of 2.1 M ammonium sulphate, 0.1 M Tris-HCl pH 8.5. Hexagonal, rod-shaped crystals grew at 20° C. and reached a maximum size of 0.05×0.05×0.3 mm after 7 days. After soaking for 3 seconds in a cryo-protection solution (2.1 M ammonium sulphate, 0.1 M Tris-HCl pH 7.2, 25% glycerol) crystals were frozen in a stream of cold nitrogen.

PDK1 in complex with staurosporine was crystallized using the hanging drop technique. Drops consisted of 1 μl PDK1 at 7.6 mg/ml, 1 μl mother liquor (2.1 M ammonium sulphate, 0.1 M Tris-HCl pH 7.2) and 0.25 μl staurosporine (10 mM in DMSO). Hexagonal shaped crystals suitable for data collection appeared after 6 weeks at 20 C. Crystals were soaked in 1.7 M ammonium sulphate, 0.1 M Tris-HCl pH 7.2, 15% glycerol and frozen in a stream of cold nitrogen.

Data Collection, Structure Solution and Refinement

Data on the PDK1-staurosporine and PDK1-UCN-01 complexes were collected at the European Synchrotron Radiation Facility (Grenoble, France) beamline ID14-EH4. The temperature of the crystals was maintained at 100 K using a nitrogen cryostream. Data were processed using the HKL package [22] with final statistics shown in Table 3. The structures were solved by rigid body refinement with CNS [23] using the previously determined PDK1 structure (See previous Examples; PDB code 1H1W) [11] as a starting model which resulted in an initial R-factor of 0.306 (R_(free)=0.284) for PDK1-staurosporine and 0.299 (R_(free)=0.311) for PDK1-UCN-01. Model building with 0 [24] and iterative refinement in CNS, including solvent molecules and the T-loop phosphorylation site, resulted in final R-factors as shown in Table 3. The ATP binding site showed well-defined density in the unbiased |F_(o)|−F_(c)|, φ_(calc) maps for all atoms of staurosporine and UCN-01, including the 7-hydroxyl group (FIG. 8). CNS topologies and coordinates for the inhibitors were generated with PRODRG [25]. No electron density could be observed for residues 51-72 (N-terminus), residues 231-239 (T-loop) and residue 359 (C-terminus) in the PDK1-UCN-01 complex. Residues 51-71 (N-terminus) and 233-238 (T-loop) were disordered in the PDK1-staurosporine complex.

Determination of Inhibition and Specificity

Protein kinase assays: PDK1 was assayed for 10 min at 30° C. in a 50 μl assay mixture in 50 mM Tris pH 7.5, 0.1 mM EGTA, 0.1% 2-mercaptoethanol, containing 100 μM PDK1tide substrate peptide (KTFCGTPEYLAPEVRREPRILSEEEQEMFRDFDYIADWC) (SEQ ID NO:112), 10 mM magnesium acetate, 100 μM [γ-³²P]ATP (200 cpm/pmole) as described previously [10]. Other protein kinases employed in Table 5, were assayed as described previously [17, 26].

Results & Discussion

Structures of the Staurosporine and UCN-01 Complexes

PDK1 (residues 51-359) was co-crystallized with staurosporine and UCN-01, and synchrotron diffraction data on a thin hexagonal needle were collected to 2.3 Å and 2.5 Å resolution, respectively.

In the unbiased |F_(o)|−F_(c)|, φ_(calc) maps well defined (>3.0σ) density could be observed in the ATP binding site of the kinase, covering all staurosporine/UCN-01 atoms including the 7-hydroxyl group (FIG. 8). After initial rounds of protein model building and inclusion of water molecules, the inhibitor molecules were built and refined with full occupancy to average B-factor of 18.5 Å² (staurosporine) and 17.3 Å² (UCN-01). Further refinement resulted in a final PDK1-staurosporine model with R=0.218 (R_(free)=0.255) and a final PDK1-UCN-01 model with R=0.184 (R_(free)=0.257), both with good stereochemistry (Table 3).

The staurosporine molecule is located in the ATP-binding site (which lies between the N-terminal and C-terminal lobes of kinases [27, 28]), at the same position described for the inhibitor in complex with the closely related (38% sequence identity) protein kinase A (PKA, [29], PDB code 1STC) (FIG. 8). Hydrophobic residues on both sides of the ATP binding cleft sandwich the heterocyclic moiety of staurosporine, namely Leu88, Val96, Ala109, Leu98 (small lobe) and Thr222, Leu212 of the larger lobe (FIG. 1).

Similar to the PKA-staurosporine complex, the lactam group mimics the interactions of the adenine base in ATP with the protein backbone, where 2 conserved hydrogen bonds are formed between the lactam-nitrogen N6 in staurosporine (nomenclature according to [30]) and the backbone-oxygen of Ser160, and the lactam-oxygen at the C5 position and the backbone-nitrogen of Ala162 (Table 4). An additional hydrogen bond is mimicked in the staurosporine sugar-moiety, where the methyl-amino group contacts oxygen O 2 of Glu166, similar to the hydrogen bond with the ribose in the PDK1-ATP complex [11], and also the backbone carbonyl of Glu209 (Table 4).

The UCN-01 molecule occupies the same position in the ATP binding site as staurosporine (maximum atomic shift=0.35 Å) (FIG. 9). The same hydrophobic interactions are made to the heterocyclic moiety in the PDK1-staurosporine complex. Hydrogen bonding interactions to the heterocycle and the sugar moiety are also conserved, with similar geometry (Table 4). However, the 7-hydroxyl group of UCN-01 forms several novel hydrogen bonds (FIG. 9, Table 4). It hydrogen bonds directly to Oγ1 of Thr222 (FIG. 9, Table 4). In addition, an ordered water molecule (B-factor=24.0 Å²) is found in a position where it contacts the 7-hydroxyl (distance=3.0 Å, Table 4) and the oxygen Oε1 of Gln220 (distance=2.5 Å) the side chain of which is shifted towards the ligand (1.5 Å for Cδ, rotation of 82° around χ₁) compared to the PDK1-STO complex. However, the water molecule is buried in a predominantly hydrophobic pocket, lined by Val143, Leu212 and Cγ2 of Thr222 (FIG. 9). Val143 also changes its position compared to the PDK1-staurosporine complex (FIG. 9), moving further towards the back of the pocket (shift of 0.7° A for the Cα carbon, and a rotation of 100° around χ₁) and displaces an ordered water molecule present in the PDK1-staurosporine complex (FIG. 9), and also observed in other kinase-staurosporine complexes [31, 30]. These changes result in more space to accommodate the bulky 7-hydroxyl group on UCN-01 as indicated by a 6° A³ increase in ligand volume (calculated with VOIDOO [32]).

Comparison with Chk1-UCN-01

High resolution data for the Chk1 kinase bound to staurosporine and UCN-01 is available (PDB code 1NVQ [30]). In Chk1, Ser147, the equivalent of Thr222 in PDK1, also hydrogen bonds the UCN-01 7-OH directly. In addition, a water mediated network of hydrogen bonds to UCN-01 is observed. However, in Chk1 the water molecule that hydrogen bonds UCN-01 occupies a different position (shifted 5.2 Å compared to the PDK1-UCN-01 complex). Chk1 appears to have a more extended hydrophilic cavity, as there are 2 additional buried water molecules present also in the Chk1-staurosporine complex. The corresponding residue to Gln220 in PDK1 is a Lys (Lys145) in Chk1, which does not interact with the ligand but points away from it.

UCN-01 Inhibition and Specificity

PDK1 inhibition by UCN-01 and staurosporine was measured using kinase assays with P³²-labelled ATP. PDK1 is inhibited by UCN-01 with an IC₅₀ value of 5 nM, and by staurosporine with an IC₅₀ of 6.5 nM. As a measure for overall specificity of UCN-01 and staurosporine, the effect of these inhibitors was tested against a panel of 29 protein kinases as described previously [17, 26]. The results are shown in Table 5 as percentage of control activity. These data further confirm that UCN-01 and staurosporine are aspecific inhibitors. UCN-01 at 1 μM concentration reduces the activity of nine kinases in the panel to less than 10%, and of ten others to below 60% of control activity. Staurosporine at 1 μM will inhibit twelve kinases to less than 10% control activity, and another ten to below 60%. Interestingly, however, several of the protein kinases were differentially inhibited by staurosporine and UCN-01 (Table 5). In an attempt to understand these differences the panel of kinases was divided in four distinct classes: (a) similar inhibition, (b) stronger inhibition by staurosporine than by UCN-01, (c) stronger inhibition by UCN-01 than by staurosporine, and (d) no inhibition (Table 5). As the additional 7-hydroxyl group is the only difference in the ligand molecules (FIG. 8), and staurosporine and UCN-01 occupy the same position with similar interactions in the binding site (FIG. 9), the residues contacting the extra hydroxyl group were identified for PDK1 and extracted from a sequence alignment of all protein kinases used in the panel (Table 5). A structure-based sequence alignment of known kinase structures was obtained from [33], which was used to validate the sequence-based sequence alignment (Table 5). The nature of the side chains lining the hydroxyl-pocket could provide a partial explanation for the relative difference between UCN-01 and staurosporine inhibition. Two trends can be observed. For the kinases that are inhibited by UCN-01, there appears to be a preference for a side chain capable of hydrogen bonding the 7-hydroxyl in the hydroxyl-pocket. This is in agreement with the presence of a Thr/Ser residue that hydrogen bonds the 7-hydroxyl in the structures of PDK1 (Thr222) and Chk1 (Ser147) bound to UCN-01. Seven out of ten kinases that are hit equally by staurosporine and UCN-01 (group (a)) appear to have a potential hydrogen bonding residue (Table 5). The kinases that are more potently inhibited by UCN-01 than by staurosporine (group (c)) contain a Thr at the Thr222 equivalent position (Table 5). Five out of nine kinases that are inhibited more potently by staurosporine than by UCN-01 (group (b)) lack a potential hydrogen binding partner in the 7-hydroxyl-pocket (Table 5).

A second trend which appears to determine specificity is the size of the residues lining the hydroxyl-pocket. If the predicted total volume of the residues (calculated with the BL-set of side chain volumes [34]) at the positions indicated in Table 5 is set against the activity in the presence of UCN-01, a correlation coefficient of 0.6 is obtained. This suggests that despite inaccuracies in this approach, such as the absence of structural information on precise side chain conformation and water molecules, a weak correlation between predicted hydroxyl pocket volume and UCN-01 inhibition exists. For instance, PKA contains a possible hydrogen bonding partner for UCN-01 (Thr183), but Met134 in the centre of the hydroxyl pocket may leave no space for the extra hydroxyl group (Table 5). A similar arrangement of residues can be observed for MAPKAP-K2 (Table 5). This size dependency may also play a role for the protein kinases neither hit by staurosporine nor UCN-01. The sequence alignment shows that the Val143 and Thr222 equivalent residues are replaced by bulkier Leu or Ile residues in several of the Mitogen Activated Protein Kinase families (Table 5). To investigate the effect of these bulkier side chains on the hydroxyl pocket, we, starting from the PDK1 crystal structure, replaced residues Val143 with Ile and Thr222 with Leu in standard side chain rotamers (in O [24]), which indeed resulted in van der Waals clashes with C7 of staurosporine (shortest distances: 2.8 Å for Leu222, 3.5 Å for Ile143), and may therefore explain the lack of susceptibility towards UCN-01 in the Mitogen Activated Protein Kinase families. CDK2 is inhibited by both staurosporine and UCN-01 similarly, however this kinase lacks a hydrogen bonding partner for the 7-hydroxyl and contains a bulky Phe (Phe80) at the Leu159 equivalent position. In a superposition of CDK2-staurosporine structure [31] with PDK1-UCN-01 (RMSD=1.3 Å on Cα atoms) staurosporine is seen to be shifted by 1.2 Å out of the potential hydroxyl pocket due to presence of the bulky Phe80. Interaction of the 7-hydroxyl on UCN-01 was described to be water mediated in CDK2 due to the lack of hydrogen bonding residues [35]. This particular example highlights the limitations of the approach described above. Other examples where none of the described effects account for the observed behaviour are AMPK and MSK1. Both MSK1 and SGK1 show the same sequence in their hydroxyl-pocket with Thr406/Thr407, respectively, as potential hydrogen bonding partners, but both were placed in different groups. MSK1 activity is abolished by 1 μM staurosporine, but shows residual activity (11%) with UCN-01. SGK1 activity is at 25% of control activity with 1 μM UCN-01, but twice as high with staurosporine.

Conclusions

UCN-01 was subjected to a specificity analysis against an in-house panel of 29 protein kinases. Contrary to the suggestions of some previous reports, the data show that UCN-01 is not a specific inhibitor as it inhibited more than half of the tested kinases at significant levels. A direct comparison with staurosporine, however, showed a different pattern of inhibition, and was the subject of further analysis. We have reported the crystal structures of PDK1 in complex with the inhibitors staurosporine and UCN-01. Both inhibitors appear to bind to PDK1 in a similar fashion compared to the Chk1-UCN-01 or PKA-staurosporine [29] complex, with additional hydrogen bonding interactions at the UCN-01 7-hydroxyl group. This moiety is hydrogen bonded directly to Thr222 and indirectly via an ordered water molecule to Gln220. A different water-mediated hydrogen bonding network is also observed in other UCN-01 complexes known to date [35, 30], and might serve as a starting point for further structure-based optimisation. The residues around the 7-hydroxyl group (“hydroxyl-pocket”) were aligned with known kinase structures and kinases sequences. It is apparent that spatial effects in the identified pocket play a key role in determining UCN-01 inhibition, as does the presence of hydrogen bonding partners for the additional hydroxyl group.

TABLE 3 Details of data collection & structure refinement. Values between brackets are for the highest resolution shell. Crystals were cryo- cooled to 100 K. All measured data were included in structure refinement. Dataset Staurosporine UCN-01 Space group P3₂21 P3₂21 Cell dimensions (Å) a = 124.17 a = 123.39 b = 124.17 b = 123.39 c = 47.31 c = 47.12 Resolution range (Å) 25-2.30 (2.38-2.30) 25-2.50 (2.59-2.50) # Observed reflections 31730 (3091) 68515 (6290) # Unique reflections 18018 (1794) 14395 (1430) Redundancy 1.8 (1.7) 4.8 (4.4) I/σI 7.5 (1.8) 4.5 (2.6) Completeness (%) 95.8 (95.8) 100.0 (99.9) R_(merge) 0.096 (0.505) 0.167 (0.688) R_(cryst), R_(free) 0.218, 0.255 0.189, 0.257 RMSD from ideal geometry Bonds (Å) 0.007 0.009 Angles (°) 1.7 1.8 B-factor RMSD (Å) 1.5 1.4 (bonded, main chain) <B> protein (Å) 31.5 27.3 <B> inhibitor (Å) 18.5 17.4

TABLE 4 Hydrogen bonding between inhibitors and PDK1. Hydrogen bonds between PDK1 and UCN-01/staurosporine (STO) were calculated with WHAT IF [36] using the HB2 algorithm [37]. This algorithm gives a 0 (no hydrogen bond) to 1 (optimal hydrogen bond) score to reflect hydrogen bond geometry (HB2 column). Donor-acceptor distances are also listed (D-A). UCN-01 UCN-01 Inhibitor Protein/H₂O D-A (Å) HB2 STO D-A (Å) STO HB2 Comment O5 N-Ala162 2.8 0.76 3.0 0.81 Conserved N6 O-Ser162 2.9 0.80 3.1 0.67 Conserved N4′ O-Glu209 3.2 0.68 3.1 0.39 Conserved N4′ Oε2-Glu166 2.6 0.63 2.5 0.45 Conserved O7 Oγ1-Thr222 3.0 0.56 7-hydroxyl O7 H₂O 3.0 0.89 Water mediated to (Oε1-Gln220)

TABLE 5 Comparison of inhibition by UCN-01 vs. staurosporine and hydroxyl pocket-lining residues. The indicated protein kinases were assayed at 0.1 mM ATP as described previously [17, 26], in the absence or presence of 1 μM staurosporine (STO) or UCN-01. Results are presented as percentage of kinase activity compared to that in control incubations. The activity results displayed in the two columns are an average of a triplicate determination. Abbreviations not defined in main text: ROCKII, Rho- dependent protein kinase-II; AMPK, AMP-activated protein kinase; MKK1, MAP-kinase kinase-1; PRAK, p38-regulated/activated protein kinase; PHK, phosphorylase kinase; CK2, Casein kinase-2; CHK1, cell cycle checkpoint kinase-1; DYRK, dual specificity tyrosine phosphorylated and regulated kinase; CSK, C-terminal Src kinase. Residues lining the hydroxyl pocket are shown in the last five columns, as derived from a multiple sequence alignment with T-Coffee [38]. Kinase STO UCN-01 Both STO and UCN-01 inhibit PDK1 5 ± 1 0 ± 1 Met134 Val143 Leu159 Gln220 Thr222 CHK1 (1NVQ [30]) 3 ± 1 1 ± 0 Ile Val Leu Lys145 Ser147 PKCα 8 ± 2 1 ± 0 Leu Thr Met Lys Ala AMPK 0 ± 0 1 ± 1 Leu Ile Met Lys Ala PHOS.KINASE (1PHK [39]) 2 ± 3 1 ± 2 Leu Ile Phe Lys Thr Lck (1QPJ [40]) 0 ± 0 3 ± 1 Met Val Thr Lys Ala CDK2/cyclin A (1AQ1 [31]) 12 ± 12 8 ± 0 Leu Val Phe80 Lys Ala PKBΔPH (1O6K [41]) 8 ± 2 9 ± 1 Leu Thr Met Lys Thr ROCK-II 9 ± 5 13 ± 2  Met Val Met Lys Ala S6K1 24 ± 8  21 ± 4  Leu Val Leu Lys Thr GSK3β (1I09 [42]) 29 ± 6  25 ± 5  Met Val Leu Lys Cys STO inhibits stronger than UCN-01 MSK1 1 ± 0 11 ± 0  Leu Val Leu Val Thr406 DYRK1α 2 ± 2 15 ± 2  Leu Met Phe Lys Val PKA (1STC [29]) 4 ± 1 27 ± 2  Leu Val Met134 Gln Thr183 MKK1 5 ± 8 53 ± 1  Leu Val Met Lys Cys MAPKAP-K2 23 ± 1  60 ± 1  His Val Met Lys Thr CSK (1BYG [43]) 25 ± 8  58 ± 3  Met Val Thr Lys Ser SAPK3/p38γ (1CM8 [44]) 37 ± 0  94 ± 8  Leu Ile Met Lys Leu SAPK4/p38δ 40 ± 5  100 ± 7  Leu Ile Met Lys Leu PRAK 48 ± 1  89 ± 4  His Val Met Lys Cys UCN-01 inhibits stronger than STO MAPKAP-K1a 18 ± 10 1 ± 1 Leu Val Leu Lys Thr341 SGK1 51 ± 4  22 ± 4  Leu Val Leu Val Thr407 Neither UCN-01 nor STO inhibits MAPK2/ERK2 (1ERK [45]) 100 ± 4  107 ± 5  Leu Ile Gln Lys Cys JNKSAPK1c 91 ± 3  112 ± 6  Met Ile Met Lys Leu SAPK2α/p38 (1P38 [46]) 76 ± 4  107 ± 5  Leu Ile Thr Lys Leu SAPK2β/p38β2 84 ± 11 106 ± 4  Leu Ile Thr Arg Leu CK2 (1F0Q [47]) 95 ± 4  102 ± 11  Leu Val Phe Arg Ile CK1 (1CKI [48]) 95 ± 11 96 ± 0  Tyr Pro Met Tyr Ile NEK6 109 ± 2  80 ± 7  Leu Ile Leu Lys Gly

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Goldsmith, The structure of mitogen-activated     protein kinase p38 at 2.1 Angstrom resolution, Proc. Natl. Acad.     Sci. USA, 94, 2327-2332 (1997). -   [47] R. Battistutta, S. Sarno, E. DeMoliner, E. Papinutto, G.     Zanotti, and L. A. Pinna, The replacement of ATP by the competitive     inhibitor emodin induces conformational modifications in the     catalytic site of protein kinase CK2, J. Biol. Chem., 275,     29618-29622 (2000). -   [48] L. M. Zhai, P. R. Graves, L. C. Robinson, M. Italiano, M. R.     Culbertson, J. Rowles, M. H. Cobb, A. A. Depaoliroach, and P. J.     Roach, Casein kinase i-gamma subfamily-molecular-cloning,     expression, and characterization of 3 mammalian isoforms and     complementation of defects in the saccharomyces-cerevisiae yck     genes, J. Biol. Chem., 270, 12717-12724 (1995). -   [49] I. Takahashi, E. Kobayashi, K. Asano, M. Yoshida, and H.     Nakano, UCN-01, a selective inhibitor of protein-kinase-c from     streptomyces, J. Antibiot., 40, 1782-1784 (1987).

Example 7 Co-Ordinates for PDK1 Fragment Co-Crystallised with Staurosporine

REMARK coordinates from restrained individual B-factor refinement REMARK refinement resolution: 25.0 - 2.30 A REMARK starting r= 0.2196 free_(— r= 0.2545) REMARK final   r= 0.2182 free_r= 0.2553 REMARK B rmsd for bonded mainchain atoms= 1.536  target= 1.5 REMARK B rmsd for bonded sidechain atoms= 2.154  target= 2.0 REMARK B rmsd for angle mainchain atoms= 2.576  target= 2.0 REMARK B rmsd for angle sidechain atoms= 3.220  target= 2.5 REMARK rweight= 0.1000 (with wa= 2.58634) REMARK target= mlf  steps= 30 REMARK sg= P3(2)21 a= 124.172 b= 124.172 c= 47.314 alpha= 90 beta= 90 gamma= 120 REMARK parameter file 1  : /dd1/david/projects/MY_CNS/prot.par REMARK parameter file 2  : /dd1/david/projects/MY_CNS/sto.par REMARK parameter file 3  : CNS_TOPPAR:water_rep.param REMARK parameter file 4  : CNS_TOPPAR:ion.param REMARK parameter file 5  : /dd1/david/projects/MY_CNS/glycerol.par REMARK molecular structure file: ../generate/alternate.mtf REMARK input coordinates: ../minimize/minimize.pdb REMARK reflection file= ../../1/hkl/cns.hkl REMARK ncs= none REMARK B-correction resolution: 6.0 - 2.30 REMARK initial B-factor correction applied to fobs : REMARK B11= −4.525 B22= −4.525 B33= 9.049 REMARK B12= −1.949 B13=   0.000 B23 = 0.000 REMARK B-factor correction applied to coordinate array B:   −0.209 REMARK bulk solvent: density level=0.340909 e/A{circumflex over ( )}3, B-factor=36.8807 A{circumflex over ( )}2 REMARK reflections with  |Fobs|/sigma_F < 0.0 rejected REMARK reflections with  |Fobs| > 1000 * rms(Fobs) rejected REMARK theoretical total number of refl. in resol. range: 18858 ( 100.0 % ) REMARK number of unobserved reflections (no entry or |F|=0):  846 ( 4.5 % ) REMARK number of reflections rejected:   0 ( 0.0 % ) REMARK total number of reflections used: 18012 ( 95.5 % ) REMARK number of reflections in working set: 17259 ( 91.5 % ) REMARK number of reflections in test set:  753 ( 4.0 % ) CRYST1  124.172  124.172  47.314  90.00  90.00  120.00  P  32  2  1 REMARK FILENAME=“bindindividual.pdb” REMARK DATE:30-Jan-2003  19:44:02 created by user: david REMARK VERSION:1.0 ATOM 1 CB PRO A 72 64.267 −7.345 13.422 1.00 74.69 A ATOM 2 CG PRO A 72 63.278 −8.432 13.027 1.00 74.97 A ATOM 3 C PRO A 72 65.866 −6.007 12.013 1.00 73.72 A ATOM 4 O PRO A 72 66.500 −6.002 10.955 1.00 73.74 A ATOM 5 N PRO A 72 64.256 −7.651 11.034 1.00 74.67 A ATOM 6 CD PRO A 72 63.762 −8.901 11.640 1.00 75.33 A ATOM 7 CA PRO A 72 64.474 −6.639 12.090 1.00 74.30 A ATOM 8 N GLN A 73 66.329 −5.474 13.141 1.00 72.17 A ATOM 9 CA GLN A 73 67.635 −4.829 13.221 1.00 70.49 A ATOM 10 CB GLN A 73 67.570 −3.424 12.611 1.00 69.71 A ATOM 11 CG GLN A 73 66.670 −2.458 13.363 1.00 68.72 A ATOM 12 CD GLN A 73 66.722 −1.054 12.795 0.00 69.01 A ATOM 13 OE1 GLN A 73 67.785 −0.435 12.735 0.00 68.92 A ATOM 14 NE2 GLN A 73 65.571 −0.541 12.376 0.00 68.92 A ATOM 15 C GLN A 73 68.057 −4.728 14.683 1.00 69.53 A ATOM 16 O GLN A 73 67.267 −5.015 15.585 1.00 69.69 A ATOM 17 N PRO A 74 69.313 −4.321 14.940 1.00 68.34 A ATOM 18 CD PRO A 74 70.411 −4.026 13.999 1.00 67.68 A ATOM 19 CA PRO A 74 69.769 −4.204 16.330 1.00 67.15 A ATOM 20 CB PRO A 74 71.198 −3.675 16.178 1.00 67.56 A ATOM 21 CG PRO A 74 71.635 −4.254 14.855 1.00 67.46 A ATOM 22 C PRO A 74 68.866 −3.240 17.105 1.00 65.27 A ATOM 23 O PRO A 74 68.496 −2.186 16.584 1.00 65.27 A ATOM 24 N ARG A 75 68.506 −3.598 18.337 1.00 62.56 A ATOM 25 CA ARG A 75 67.642 −2.730 19.136 1.00 59.53 A ATOM 26 CB ARG A 75 67.543 −3.228 20.582 1.00 62.40 A ATOM 27 CG ARG A 75 66.120 −3.565 21.023 1.00 64.22 A ATOM 28 CD ARG A 75 66.020 −3.746 22.537 1.00 66.65 A ATOM 29 NE ARG A 75 64.741 −4.332 22.943 1.00 68.76 A ATOM 30 CZ ARG A 75 64.390 −4.572 24.204 1.00 70.18 A ATOM 31 NH1 ARG A 75 65.218 −4.272 25.197 1.00 70.31 A ATOM 32 NH2 ARG A 75 63.213 −5.125 24.477 1.00 71.64 A ATOM 33 C ARG A 75 68.184 −1.306 19.126 1.00 55.61 A ATOM 34 O ARG A 75 69.386 −1.082 18.961 1.00 55.58 A ATOM 35 N LYS A 76 67.294 −0.341 19.295 1.00 50.06 A ATOM 36 CA LYS A 76 67.704 1.050 19.297 1.00 45.50 A ATOM 37 CB LYS A 76 66.498 1.941 19.594 1.00 45.42 A ATOM 38 CG LYS A 76 66.404 3.192 18.735 1.00 45.70 A ATOM 39 CD LYS A 76 66.329 2.829 17.257 1.00 44.53 A ATOM 40 CE LYS A 76 66.030 4.045 16.396 1.00 44.45 A ATOM 41 NZ LYS A 76 66.091 3.733 14.939 1.00 43.30 A ATOM 42 C LYS A 76 68.783 1.251 20.359 1.00 42.73 A ATOM 43 O LYS A 76 68.715 0.681 21.447 1.00 42.46 A ATOM 44 N LYS A 77 69.793 2.046 20.038 1.00 39.63 A ATOM 45 CA LYS A 77 70.851 2.309 20.995 1.00 36.33 A ATOM 46 CB LYS A 77 72.139 2.670 20.267 1.00 36.33 A ATOM 47 CG LYS A 77 72.655 1.570 19.353 1.00 36.55 A ATOM 48 CD LYS A 77 74.005 1.945 18.785 1.00 35.61 A ATOM 49 CE LYS A 77 74.491 0.932 17.766 1.00 38.34 A ATOM 50 NZ LYS A 77 74.706 −0.419 18.354 1.00 38.65 A ATOM 51 C LYS A 77 70.413 3.459 21.889 1.00 35.52 A ATOM 52 O LYS A 77 69.475 4.190 21.557 1.00 32.62 A ATOM 53 N ARG A 78 71.097 3.608 23.020 1.00 34.95 A ATOM 54 CA ARG A 78 70.801 4.654 23.991 1.00 33.79 A ATOM 55 CB ARG A 78 69.917 4.094 25.114 1.00 35.78 A ATOM 56 CG ARG A 78 70.211 2.652 25.483 1.00 38.18 A ATOM 57 CD ARG A 78 69.036 2.040 26.239 1.00 38.81 A ATOM 58 NE ARG A 78 68.995 0.578 26.160 0.00 38.43 A ATOM 59 CZ ARG A 78 69.889 −0.232 26.719 0.00 38.44 A ATOM 60 NH1 ARG A 78 70.906 0.274 27.401 0.00 38.37 A ATOM 61 NH2 ARG A 78 69.760 −1.549 26.610 0.00 38.37 A ATOM 62 C ARG A 78 72.099 5.230 24.544 1.00 31.96 A ATOM 63 O ARG A 78 73.133 4.576 24.515 1.00 32.75 A ATOM 64 N PRO A 79 72.060 6.470 25.055 1.00 30.51 A ATOM 65 CD PRO A 79 70.844 7.272 25.274 1.00 27.35 A ATOM 66 CA PRO A 79 73.236 7.150 25.611 1.00 29.82 A ATOM 67 CB PRO A 79 72.626 8.326 26.365 1.00 28.52 A ATOM 68 CG PRO A 79 71.418 8.628 25.559 1.00 29.89 A ATOM 69 C PRO A 79 74.129 6.298 26.510 1.00 30.92 A ATOM 70 O PRO A 79 75.356 6.357 26.412 1.00 33.32 A ATOM 71 N GLU A 80 73.516 5.510 27.383 1.00 29.85 A ATOM 72 CA GLU A 80 74.273 4.677 28.300 1.00 31.98 A ATOM 73 CB GLU A 80 73.327 3.941 29.242 1.00 34.31 A ATOM 74 CG GLU A 80 72.697 2.710 28.622 1.00 41.92 A ATOM 75 CD GLU A 80 71.205 2.626 28.872 1.00 44.52 A ATOM 76 OE1 GLU A 80 70.461 3.466 28.317 1.00 46.38 A ATOM 77 OE2 GLU A 80 70.780 1.721 29.625 1.00 46.03 A ATOM 78 C GLU A 80 75.157 3.663 27.578 1.00 30.62 A ATOM 79 O GLU A 80 76.101 3.144 28.170 1.00 30.21 A ATOM 80 N ASP A 81 74.859 3.378 26.312 1.00 28.14 A ATOM 81 CA ASP A 81 75.659 2.417 25.548 1.00 27.32 A ATOM 82 CB ASP A 81 74.938 1.990 24.253 1.00 27.75 A ATOM 83 CG ASP A 81 73.612 1.275 24.512 1.00 30.45 A ATOM 84 OD1 ASP A 81 73.495 0.549 25.525 1.00 30.76 A ATOM 85 OD2 ASP A 81 72.686 1.424 23.686 1.00 30.74 A ATOM 86 C ASP A 81 77.026 2.990 25.166 1.00 26.35 A ATOM 87 O ASP A 81 77.895 2.266 24.680 1.00 25.33 A ATOM 88 N PHE A 82 77.217 4.283 25.404 1.00 24.95 A ATOM 89 CA PHE A 82 78.457 4.948 25.035 1.00 23.57 A ATOM 90 CB PHE A 82 78.168 6.040 23.991 1.00 23.02 A ATOM 91 CG PHE A 82 77.507 5.534 22.742 1.00 23.64 A ATOM 92 CD1 PHE A 82 78.270 5.059 21.680 1.00 23.15 A ATOM 93 CD2 PHE A 82 76.123 5.504 22.640 1.00 23.41 A ATOM 94 CE1 PHE A 82 77.670 4.559 20.540 1.00 23.43 A ATOM 95 CE2 PHE A 82 75.504 5.003 21.498 1.00 24.29 A ATOM 96 CZ PHE A 82 76.283 4.527 20.444 1.00 25.15 A ATOM 97 C PHE A 82 79.199 5.609 26.186 1.00 24.39 A ATOM 98 O PHE A 82 78.647 5.847 27.259 1.00 22.78 A ATOM 99 N LYS A 83 80.471 5.896 25.932 1.00 22.40 A ATOM 100 CA LYS A 83 81.294 6.615 26.869 1.00 23.38 A ATOM 101 CB LYS A 83 82.554 5.834 27.250 1.00 24.29 A ATOM 102 CG LYS A 83 83.453 6.594 28.227 1.00 27.32 A ATOM 103 CD LYS A 83 84.411 5.675 28.988 1.00 31.40 A ATOM 104 CE LYS A 83 85.321 4.906 28.044 0.00 30.06 A ATOM 105 NZ LYS A 83 86.145 5.819 27.207 0.00 30.54 A ATOM 106 C LYS A 83 81.656 7.847 26.046 1.00 24.47 A ATOM 107 O LYS A 83 82.518 7.787 25.162 1.00 26.09 A ATOM 108 N PHE A 84 80.965 8.951 26.309 1.00 21.59 A ATOM 109 CA PHE A 84 81.211 10.182 25.583 1.00 21.61 A ATOM 110 CB PHE A 84 80.073 11.169 25.811 1.00 20.62 A ATOM 111 CG PHE A 84 78.794 10.757 25.159 1.00 20.05 A ATOM 112 CD1 PHE A 84 77.915 9.905 25.805 1.00 18.27 A ATOM 113 CD2 PHE A 84 78.498 11.176 23.868 1.00 19.96 A ATOM 114 CE1 PHE A 84 76.764 9.473 25.183 1.00 19.47 A ATOM 115 CE2 PHE A 84 77.346 10.748 23.233 1.00 21.09 A ATOM 116 CZ PHE A 84 76.475 9.894 23.890 1.00 20.64 A ATOM 117 C PHE A 84 82.525 10.820 25.966 1.00 22.27 A ATOM 118 O PHE A 84 82.900 10.822 27.129 1.00 24.09 A ATOM 119 N GLY A 85 83.213 11.371 24.972 1.00 22.72 A ATOM 120 CA GLY A 85 84.496 12.007 25.203 1.00 22.66 A ATOM 121 C GLY A 85 84.540 13.481 24.839 1.00 22.72 A ATOM 122 O GLY A 85 83.622 14.228 25.158 1.00 22.51 A ATOM 123 N LYS A 86 85.608 13.894 24.162 1.00 22.49 A ATOM 124 CA LYS A 86 85.794 15.291 23.784 1.00 22.53 A ATOM 125 CB LYS A 86 87.238 15.530 23.333 1.00 24.44 A ATOM 126 CG LYS A 86 87.617 14.804 22.051 1.00 26.94 A ATOM 127 CD LYS A 86 89.033 15.120 21.594 1.00 29.52 A ATOM 128 CE LYS A 86 89.166 16.571 21.154 1.00 35.93 A ATOM 129 NZ LYS A 86 90.505 16.892 20.553 1.00 38.21 A ATOM 130 C LYS A 86 84.857 15.798 22.699 1.00 23.09 A ATOM 131 O LYS A 86 84.295 15.032 21.923 1.00 22.85 A ATOM 132 N ILE A 87 84.702 17.114 22.664 1.00 22.28 A ATOM 133 CA ILE A 87 83.867 17.780 21.683 1.00 21.22 A ATOM 134 CB ILE A 87 83.429 19.170 22.204 1.00 22.05 A ATOM 135 CG2 ILE A 87 82.792 19.993 21.076 1.00 17.65 A ATOM 136 CG1 ILE A 87 82.493 18.998 23.406 1.00 21.65 A ATOM 137 CD1 ILE A 87 82.159 20.300 24.118 1.00 18.47 A ATOM 138 C ILE A 87 84.707 17.963 20.418 1.00 21.83 A ATOM 139 O ILE A 87 85.782 18.543 20.470 1.00 21.99 A ATOM 140 N LEU A 88 84.226 17.463 19.288 1.00 22.57 A ATOM 141 CA LEU A 88 84.964 17.614 18.039 1.00 22.76 A ATOM 142 CB LEU A 88 84.586 16.515 17.044 1.00 20.65 A ATOM 143 CG LEU A 88 84.899 15.107 17.535 1.00 20.09 A ATOM 144 CD1 LEU A 88 84.455 14.082 16.502 1.00 17.42 A ATOM 145 CD2 LEU A 88 86.392 15.004 17.813 1.00 17.76 A ATOM 146 C LEU A 88 84.657 18.964 17.428 1.00 23.53 A ATOM 147 O LEU A 88 85.512 19.577 16.794 1.00 24.73 A ATOM 148 N GLY A 89 83.430 19.428 17.619 1.00 24.20 A ATOM 149 CA GLY A 89 83.057 20.710 17.062 1.00 28.57 A ATOM 150 C GLY A 89 81.649 21.131 17.431 1.00 32.57 A ATOM 151 O GLY A 89 80.834 20.318 17.882 1.00 32.78 A ATOM 152 N GLU A 90 81.363 22.412 17.224 1.00 35.17 A ATOM 153 CA GLU A 90 80.063 22.964 17.542 1.00 39.17 A ATOM 154 CB GLU A 90 80.168 23.853 18.784 1.00 41.47 A ATOM 155 CG GLU A 90 80.112 23.061 20.082 1.00 47.18 A ATOM 156 CD GLU A 90 80.422 23.893 21.313 1.00 50.49 A ATOM 157 OE1 GLU A 90 81.610 24.228 21.526 1.00 51.41 A ATOM 158 OE2 GLU A 90 79.476 24.210 22.067 1.00 53.44 A ATOM 159 C GLU A 90 79.436 23.743 16.402 1.00 40.69 A ATOM 160 O GLU A 90 80.110 24.185 15.471 1.00 40.64 A ATOM 161 N GLY A 91 78.121 23.881 16.488 1.00 42.58 A ATOM 162 CA GLY A 91 77.363 24.618 15.503 1.00 43.40 A ATOM 163 C GLY A 91 76.303 25.335 16.306 1.00 44.83 A ATOM 164 O GLY A 91 76.154 25.083 17.507 1.00 43.64 A ATOM 165 N SER A 92 75.579 26.244 15.669 1.00 47.22 A ATOM 166 CA SER A 92 74.522 26.969 16.366 1.00 48.94 A ATOM 167 CB SER A 92 73.961 28.066 15.461 1.00 51.50 A ATOM 168 OG SER A 92 73.663 27.541 14.175 1.00 54.98 A ATOM 169 C SER A 92 73.454 25.928 16.625 1.00 47.87 A ATOM 170 O SER A 92 72.745 25.950 17.635 1.00 47.78 A ATOM 171 N PHE A 93 73.392 24.994 15.689 1.00 46.49 A ATOM 172 CA PHE A 93 72.434 23.909 15.697 1.00 46.02 A ATOM 173 CB PHE A 93 72.297 23.369 14.263 1.00 49.54 A ATOM 174 CG PHE A 93 73.588 23.398 13.459 1.00 50.29 A ATOM 175 CD1 PHE A 93 74.301 22.229 13.209 1.00 52.29 A ATOM 176 CD2 PHE A 93 74.058 24.593 12.915 1.00 51.94 A ATOM 177 CE1 PHE A 93 75.459 22.245 12.424 1.00 52.28 A ATOM 178 CE2 PHE A 93 75.209 24.622 12.135 1.00 52.58 A ATOM 179 CZ PHE A 93 75.911 23.443 11.887 1.00 53.99 A ATOM 180 C PHE A 93 72.700 22.754 16.662 1.00 43.48 A ATOM 181 O PHE A 93 71.772 22.245 17.292 1.00 42.15 A ATOM 182 N SER A 94 73.955 22.343 16.796 1.00 39.99 A ATOM 183 CA SER A 94 74.245 21.206 17.655 1.00 36.12 A ATOM 184 CB SER A 94 73.839 19.937 16.921 1.00 38.79 A ATOM 185 OG SER A 94 74.549 19.863 15.695 1.00 40.39 A ATOM 186 C SER A 94 75.697 21.066 18.083 1.00 32.29 A ATOM 187 O SER A 94 76.513 21.962 17.890 1.00 30.04 A ATOM 188 N THR A 95 76.006 19.909 18.655 1.00 28.50 A ATOM 189 CA THR A 95 77.350 19.614 19.116 1.00 26.86 A ATOM 190 CB THR A 95 77.432 19.642 20.652 1.00 27.90 A ATOM 191 OG1 THR A 95 76.907 20.882 21.136 1.00 32.56 A ATOM 192 CG2 THR A 95 78.874 19.502 21.112 1.00 27.77 A ATOM 193 C THR A 95 77.757 18.225 18.653 1.00 23.70 A ATOM 194 O THR A 95 76.971 17.287 18.724 1.00 24.35 A ATOM 195 N VAL A 96 78.991 18.100 18.184 1.00 22.75 A ATOM 196 CA VAL A 96 79.505 16.813 17.733 1.00 20.60 A ATOM 197 CB VAL A 96 80.139 16.909 16.336 1.00 17.79 A ATOM 198 CG1 VAL A 96 80.625 15.530 15.898 1.00 18.21 A ATOM 199 CG2 VAL A 96 79.131 17.447 15.344 1.00 13.79 A ATOM 200 C VAL A 96 80.566 16.351 18.716 1.00 21.23 A ATOM 201 O VAL A 96 81.600 17.006 18.889 1.00 22.12 A ATOM 202 N VAL A 97 80.310 15.220 19.362 1.00 22.06 A ATOM 203 CA VAL A 97 81.244 14.690 20.345 1.00 24.07 A ATOM 204 CB VAL A 97 80.592 14.680 21.743 1.00 24.91 A ATOM 205 CG1 VAL A 97 79.199 14.124 21.649 1.00 28.97 A ATOM 206 CG2 VAL A 97 81.422 13.859 22.715 1.00 27.97 A ATOM 207 C VAL A 97 81.748 13.298 20.002 1.00 23.47 A ATOM 208 O VAL A 97 81.017 12.491 19.436 1.00 26.62 A ATOM 209 N LEU A 98 83.007 13.024 20.329 1.00 22.92 A ATOM 210 CA LEU A 98 83.586 11.713 20.063 1.00 23.27 A ATOM 211 CB LEU A 98 85.117 11.777 20.110 1.00 21.94 A ATOM 212 CG LEU A 98 85.932 10.495 19.854 1.00 22.83 A ATOM 213 CD1 LEU A 98 85.606 9.924 18.486 1.00 23.24 A ATOM 214 CD2 LEU A 98 87.422 10.802 19.945 1.00 21.21 A ATOM 215 C LEU A 98 83.069 10.782 21.144 1.00 23.95 A ATOM 216 O LEU A 98 83.143 11.099 22.322 1.00 26.02 A ATOM 217 N ALA A 99 82.523 9.645 20.738 1.00 24.41 A ATOM 218 CA ALA A 99 81.999 8.677 21.686 1.00 23.76 A ATOM 219 CB ALA A 99 80.485 8.692 21.668 1.00 20.64 A ATOM 220 C ALA A 99 82.502 7.282 21.357 1.00 26.42 A ATOM 221 O ALA A 99 82.792 6.951 20.195 1.00 26.78 A ATOM 222 N ARG A 100 82.602 6.462 22.394 1.00 26.77 A ATOM 223 CA ARG A 100 83.055 5.094 22.238 1.00 26.80 A ATOM 224 CB ARG A 100 84.362 4.897 23.001 1.00 28.29 A ATOM 225 CG ARG A 100 84.967 3.522 22.853 1.00 33.87 A ATOM 226 CD ARG A 100 86.281 3.447 23.617 1.00 38.01 A ATOM 227 NE ARG A 100 87.337 4.240 22.983 1.00 41.22 A ATOM 228 CZ ARG A 100 87.932 3.917 21.837 1.00 41.46 A ATOM 229 NH1 ARG A 100 87.580 2.813 21.190 1.00 41.28 A ATOM 230 NH2 ARG A 100 88.887 4.692 21.339 1.00 43.39 A ATOM 231 C ARG A 100 81.970 4.167 22.770 1.00 24.32 A ATOM 232 O ARG A 100 81.583 4.251 23.934 1.00 25.42 A ATOM 233 N GLU A 101 81.456 3.308 21.900 1.00 22.41 A ATOM 234 CA GLU A 101 80.417 2.367 22.281 1.00 22.87 A ATOM 235 CB GLU A 101 79.787 1.775 21.025 1.00 21.96 A ATOM 236 CG GLU A 101 78.819 0.652 21.292 1.00 24.68 A ATOM 237 CD GLU A 101 78.203 0.137 20.018 1.00 28.27 A ATOM 238 OE1 GLU A 101 78.965 −0.113 19.057 1.00 28.96 A ATOM 239 OE2 GLU A 101 76.963 −0.022 19.971 1.00 29.77 A ATOM 240 C GLU A 101 81.015 1.261 23.151 1.00 23.59 A ATOM 241 O GLU A 101 81.945 0.574 22.738 1.00 24.80 A ATOM 242 N LEU A 102 80.475 1.088 24.351 1.00 26.09 A ATOM 243 CA LEU A 102 80.982 0.083 25.289 1.00 28.74 A ATOM 244 CB LEU A 102 80.173 0.110 26.593 1.00 30.16 A ATOM 245 CG LEU A 102 80.347 1.308 27.532 1.00 34.19 A ATOM 246 CD1 LEU A 102 81.824 1.692 27.599 1.00 33.27 A ATOM 247 CD2 LEU A 102 79.527 2.477 27.046 1.00 34.46 A ATOM 248 C LEU A 102 81.042 −1.359 24.791 1.00 28.32 A ATOM 249 O LEU A 102 82.067 −2.024 24.916 1.00 29.83 A ATOM 250 N ALA A 103 79.948 −1.841 24.226 1.00 27.34 A ATOM 251 CA ALA A 103 79.887 −3.218 23.763 1.00 27.81 A ATOM 252 CB ALA A 103 78.466 −3.549 23.367 1.00 27.48 A ATOM 253 C ALA A 103 80.828 −3.593 22.624 1.00 27.42 A ATOM 254 O ALA A 103 81.172 −4.765 22.463 1.00 28.68 A ATOM 255 N THR A 104 81.257 −2.612 21.842 1.00 24.97 A ATOM 256 CA THR A 104 82.105 −2.907 20.695 1.00 23.79 A ATOM 257 CB THR A 104 81.441 −2.472 19.393 1.00 22.01 A ATOM 258 OG1 THR A 104 81.355 −1.041 19.379 1.00 23.91 A ATOM 259 CG2 THR A 104 80.051 −3.069 19.261 1.00 17.30 A ATOM 260 C THR A 104 83.444 −2.221 20.712 1.00 25.00 A ATOM 261 O THR A 104 84.350 −2.616 19.972 1.00 25.02 A ATOM 262 N SER A 105 83.551 −1.172 21.525 1.00 24.89 A ATOM 263 CA SER A 105 84.775 −0.394 21.616 1.00 24.55 A ATOM 264 CB SER A 105 85.979 −1.334 21.732 1.00 26.36 A ATOM 265 OG SER A 105 87.143 −0.621 22.090 1.00 32.45 A ATOM 266 C SER A 105 84.916 0.514 20.374 1.00 23.38 A ATOM 267 O SER A 105 85.931 1.175 20.188 1.00 24.92 A ATOM 268 N ARG A 106 83.888 0.546 19.531 1.00 20.51 A ATOM 269 CA ARG A 106 83.906 1.372 18.323 1.00 19.31 A ATOM 270 CB ARG A 106 82.778 0.947 17.370 1.00 19.05 A ATOM 271 CG ARG A 106 83.099 −0.283 16.520 1.00 15.69 A ATOM 272 CD ARG A 106 81.853 −0.804 15.832 1.00 19.45 A ATOM 273 NE ARG A 106 82.144 −1.838 14.846 1.00 20.98 A ATOM 274 CZ ARG A 106 81.234 −2.673 14.354 1.00 21.77 A ATOM 275 NH1 ARG A 106 79.974 −2.599 14.768 1.00 19.65 A ATOM 276 NH2 ARG A 106 81.577 −3.560 13.427 1.00 21.43 A ATOM 277 C ARG A 106 83.760 2.858 18.624 1.00 17.84 A ATOM 278 O ARG A 106 83.022 3.234 19.525 1.00 15.87 A ATOM 279 N GLU A 107 84.463 3.691 17.863 1.00 18.23 A ATOM 280 CA GLU A 107 84.395 5.144 18.039 1.00 22.75 A ATOM 281 CB GLU A 107 85.773 5.800 17.929 1.00 23.58 A ATOM 282 CG GLU A 107 86.828 5.254 18.859 1.00 32.15 A ATOM 283 CD GLU A 107 88.066 6.131 18.878 1.00 35.04 A ATOM 284 OE1 GLU A 107 88.145 7.019 19.755 1.00 36.99 A ATOM 285 OE2 GLU A 107 88.949 5.944 18.007 1.00 37.54 A ATOM 286 C GLU A 107 83.514 5.787 16.982 1.00 21.00 A ATOM 287 O GLU A 107 83.709 5.577 15.787 1.00 21.37 A ATOM 288 N TYR A 108 82.570 6.593 17.437 1.00 19.48 A ATOM 289 CA TYR A 108 81.652 7.298 16.559 1.00 18.30 A ATOM 290 CB TYR A 108 80.228 6.791 16.754 1.00 17.52 A ATOM 291 CG TYR A 108 79.993 5.373 16.309 1.00 22.75 A ATOM 292 CD1 TYR A 108 79.727 5.075 14.972 1.00 20.94 A ATOM 293 CE1 TYR A 108 79.492 3.765 14.571 1.00 23.91 A ATOM 294 CD2 TYR A 108 80.019 4.324 17.231 1.00 19.41 A ATOM 295 CE2 TYR A 108 79.788 3.026 16.845 1.00 19.33 A ATOM 296 CZ TYR A 108 79.527 2.744 15.521 1.00 23.13 A ATOM 297 OH TYR A 108 79.333 1.438 15.143 1.00 23.65 A ATOM 298 C TYR A 108 81.660 8.777 16.906 1.00 18.00 A ATOM 299 O TYR A 108 81.929 9.161 18.046 1.00 18.12 A ATOM 300 N ALA A 109 81.370 9.603 15.912 1.00 17.20 A ATOM 301 CA ALA A 109 81.274 11.036 16.114 1.00 15.30 A ATOM 302 CB ALA A 109 81.853 11.784 14.928 1.00 13.44 A ATOM 303 C ALA A 109 79.759 11.205 16.178 1.00 17.20 A ATOM 304 O ALA A 109 79.056 11.019 15.179 1.00 17.23 A ATOM 305 N ILE A 110 79.250 11.522 17.362 1.00 17.40 A ATOM 306 CA ILE A 110 77.814 11.654 17.542 1.00 17.60 A ATOM 307 CB ILE A 110 77.380 10.957 18.842 1.00 16.56 A ATOM 308 CG2 ILE A 110 75.906 11.236 19.119 1.00 14.97 A ATOM 309 CG1 ILE A 110 77.672 9.453 18.728 1.00 14.02 A ATOM 310 CD1 ILE A 110 77.197 8.632 19.907 1.00 11.93 A ATOM 311 C ILE A 110 77.306 13.089 17.548 1.00 19.83 A ATOM 312 O ILE A 110 77.690 13.892 18.396 1.00 20.84 A ATOM 313 N LYS A 111 76.444 13.415 16.597 1.00 18.58 A ATOM 314 CA LYS A 111 75.902 14.761 16.551 1.00 20.88 A ATOM 315 CB LYS A 111 75.455 15.115 15.131 1.00 21.39 A ATOM 316 CG LYS A 111 75.016 16.558 14.975 1.00 24.84 A ATOM 317 CD LYS A 111 75.005 16.971 13.516 1.00 27.43 A ATOM 318 CE LYS A 111 74.426 18.359 13.343 1.00 28.44 A ATOM 319 NZ LYS A 111 74.619 18.871 11.972 1.00 28.27 A ATOM 320 C LYS A 111 74.724 14.819 17.507 1.00 20.66 A ATOM 321 O LYS A 111 73.797 14.008 17.410 1.00 20.23 A ATOM 322 N ILE A 112 74.772 15.765 18.441 1.00 20.09 A ATOM 323 CA ILE A 112 73.704 15.914 19.426 1.00 23.02 A ATOM 324 CB ILE A 112 74.261 15.882 20.863 1.00 24.20 A ATOM 325 CG2 ILE A 112 73.116 15.765 21.864 1.00 21.42 A ATOM 326 CG1 ILE A 112 75.206 14.692 21.023 1.00 24.14 A ATOM 327 CD1 ILE A 112 75.893 14.634 22.375 1.00 26.83 A ATOM 328 C ILE A 112 72.962 17.225 19.221 1.00 22.53 A ATOM 329 O ILE A 112 73.573 18.286 19.132 1.00 21.31 A ATOM 330 N LEU A 113 71.641 17.138 19.150 1.00 24.04 A ATOM 331 CA LEU A 113 70.800 18.313 18.940 1.00 25.81 A ATOM 332 CB LEU A 113 70.135 18.264 17.555 1.00 24.66 A ATOM 333 CG LEU A 113 70.988 18.095 16.295 1.00 26.73 A ATOM 334 CD1 LEU A 113 71.316 16.620 16.093 1.00 24.51 A ATOM 335 CD2 LEU A 113 70.234 18.637 15.083 1.00 26.16 A ATOM 336 C LEU A 113 69.702 18.400 19.994 1.00 27.62 A ATOM 337 O LEU A 113 69.053 17.398 20.314 1.00 29.70 A ATOM 338 N GLU A 114 69.491 19.597 20.530 1.00 29.32 A ATOM 339 CA GLU A 114 68.445 19.806 21.526 1.00 31.56 A ATOM 340 CB GLU A 114 68.775 21.020 22.391 1.00 34.85 A ATOM 341 CG GLU A 114 67.680 21.357 23.392 1.00 42.32 A ATOM 342 CD GLU A 114 67.922 22.670 24.108 1.00 45.56 A ATOM 343 OE1 GLU A 114 68.086 23.700 23.417 1.00 48.01 A ATOM 344 OE2 GLU A 114 67.941 22.673 25.359 1.00 48.10 A ATOM 345 C GLU A 114 67.107 20.036 20.816 1.00 31.02 A ATOM 346 O GLU A 114 66.926 21.049 20.140 1.00 30.39 A ATOM 347 N LYS A 115 66.176 19.099 20.967 1.00 30.58 A ATOM 348 CA LYS A 115 64.872 19.218 20.321 1.00 31.63 A ATOM 349 CB LYS A 115 63.964 18.049 20.734 1.00 28.91 A ATOM 350 CG LYS A 115 64.287 16.742 20.003 1.00 28.07 A ATOM 351 CD LYS A 115 63.356 15.580 20.368 1.00 23.95 A ATOM 352 CE LYS A 115 63.713 14.960 21.707 1.00 23.89 A ATOM 353 NZ LYS A 115 62.860 13.782 22.020 1.00 24.15 A ATOM 354 C LYS A 115 64.165 20.551 20.591 1.00 33.78 A ATOM 355 O LYS A 115 63.495 21.100 19.711 1.00 33.61 A ATOM 356 N ARG A 116 64.325 21.076 21.801 1.00 35.55 A ATOM 357 CA ARG A 116 63.682 22.332 22.176 1.00 38.66 A ATOM 358 CB ARG A 116 63.932 22.627 23.663 1.00 42.20 A ATOM 359 CG ARG A 116 62.949 23.603 24.302 1.00 47.35 A ATOM 360 CD ARG A 116 63.670 24.685 25.109 1.00 52.44 A ATOM 361 NE ARG A 116 64.526 24.141 26.166 1.00 56.30 A ATOM 362 CZ ARG A 116 64.142 23.920 27.423 1.00 57.97 A ATOM 363 NH1 ARG A 116 62.899 24.199 27.808 1.00 58.89 A ATOM 364 NH2 ARG A 116 65.006 23.420 28.300 1.00 56.55 A ATOM 365 C ARG A 116 64.227 23.472 21.323 1.00 37.67 A ATOM 366 O ARG A 116 63.474 24.246 20.735 1.00 36.66 A ATOM 367 N HIS A 117 65.550 23.555 21.259 1.00 37.78 A ATOM 368 CA HIS A 117 66.236 24.590 20.501 1.00 35.88 A ATOM 369 CB HIS A 117 67.744 24.417 20.676 1.00 35.60 A ATOM 370 CG HIS A 117 68.560 25.532 20.101 1.00 37.06 A ATOM 371 CD2 HIS A 117 69.508 25.535 19.134 1.00 38.11 A ATOM 372 ND1 HIS A 117 68.469 26.831 20.550 1.00 37.56 A ATOM 373 CE1 HIS A 117 69.325 27.587 19.886 1.00 38.35 A ATOM 374 NE2 HIS A 117 69.969 26.825 19.021 1.00 38.67 A ATOM 375 C HIS A 117 65.859 24.529 19.024 1.00 34.83 A ATOM 376 O HIS A 117 65.600 25.554 18.398 1.00 35.80 A ATOM 377 N ILE A 118 65.827 23.321 18.474 1.00 33.01 A ATOM 378 CA ILE A 118 65.483 23.122 17.071 1.00 32.12 A ATOM 379 CB ILE A 118 65.575 21.629 16.692 1.00 33.37 A ATOM 380 CG2 ILE A 118 64.968 21.398 15.312 1.00 33.44 A ATOM 381 CG1 ILE A 118 67.032 21.168 16.732 1.00 33.47 A ATOM 382 CD1 ILE A 118 67.195 19.685 16.479 1.00 35.01 A ATOM 383 C ILE A 118 64.066 23.603 16.760 1.00 31.17 A ATOM 384 O ILE A 118 63.838 24.295 15.774 1.00 29.39 A ATOM 385 N ILE A 119 63.117 23.209 17.600 1.00 31.17 A ATOM 386 CA ILE A 119 61.725 23.590 17.420 1.00 31.73 A ATOM 387 CB ILE A 119 60.841 22.896 18.473 1.00 31.45 A ATOM 388 CG2 ILE A 119 59.471 23.560 18.548 1.00 26.98 A ATOM 389 CG1 ILE A 119 60.735 21.409 18.131 1.00 27.55 A ATOM 390 CD1 ILE A 119 60.092 20.574 19.205 1.00 26.52 A ATOM 391 C ILE A 119 61.549 25.100 17.519 1.00 33.53 A ATOM 392 O ILE A 119 60.879 25.714 16.688 1.00 32.81 A ATOM 393 N ALA A 120 62.165 25.691 18.535 1.00 34.30 A ATOM 394 CA ALA A 120 62.078 27.125 18.749 1.00 34.63 A ATOM 395 CB ALA A 120 62.811 27.506 20.029 1.00 35.03 A ATOM 396 C ALA A 120 62.657 27.889 17.574 1.00 35.68 A ATOM 397 O ALA A 120 62.141 28.938 17.195 1.00 36.85 A ATOM 398 N GLU A 121 63.732 27.369 16.995 1.00 35.66 A ATOM 399 CA GLU A 121 64.375 28.041 15.870 1.00 36.43 A ATOM 400 CB GLU A 121 65.873 27.726 15.864 1.00 40.99 A ATOM 401 CG GLU A 121 66.637 28.166 17.116 1.00 45.01 A ATOM 402 CD GLU A 121 66.844 29.676 17.205 1.00 48.12 A ATOM 403 OE1 GLU A 121 67.670 30.104 18.043 1.00 49.33 A ATOM 404 OE2 GLU A 121 66.188 30.433 16.451 1.00 49.20 A ATOM 405 C GLU A 121 63.780 27.670 14.512 1.00 34.98 A ATOM 406 O GLU A 121 64.282 28.105 13.480 1.00 34.50 A ATOM 407 N ASN A 122 62.716 26.869 14.517 1.00 33.68 A ATOM 408 CA ASN A 122 62.060 26.434 13.286 1.00 32.99 A ATOM 409 CB ASN A 122 61.492 27.639 12.530 1.00 35.58 A ATOM 410 CG ASN A 122 60.424 28.373 13.315 1.00 38.88 A ATOM 411 OD1 ASN A 122 60.717 29.154 14.227 1.00 38.30 A ATOM 412 ND2 ASN A 122 59.170 28.116 12.970 1.00 38.77 A ATOM 413 C ASN A 122 63.024 25.679 12.367 1.00 31.80 A ATOM 414 O ASN A 122 63.095 25.957 11.172 1.00 30.78 A ATOM 415 N LYS A 123 63.754 24.716 12.919 1.00 29.93 A ATOM 416 CA LYS A 123 64.717 23.966 12.120 1.00 29.87 A ATOM 417 CB LYS A 123 66.100 24.016 12.775 1.00 30.75 A ATOM 418 CG LYS A 123 66.669 25.406 12.895 1.00 33.94 A ATOM 419 CD LYS A 123 66.810 26.049 11.527 1.00 37.59 A ATOM 420 CE LYS A 123 67.354 27.466 11.646 1.00 39.07 A ATOM 421 NZ LYS A 123 67.460 28.121 10.310 1.00 41.71 A ATOM 422 C LYS A 123 64.337 22.514 11.880 1.00 27.38 A ATOM 423 O LYS A 123 65.139 21.745 11.355 1.00 24.93 A ATOM 424 N VAL A 124 63.124 22.132 12.260 1.00 24.22 A ATOM 425 CA VAL A 124 62.716 20.756 12.062 1.00 22.73 A ATOM 426 CB VAL A 124 61.235 20.559 12.416 1.00 22.36 A ATOM 427 CG1 VAL A 124 60.794 19.146 12.064 1.00 22.84 A ATOM 428 CG2 VAL A 124 61.031 20.802 13.905 1.00 20.63 A ATOM 429 C VAL A 124 62.981 20.320 10.623 1.00 23.50 A ATOM 430 O VAL A 124 63.633 19.297 10.385 1.00 21.86 A ATOM 431 N PRO A 125 62.512 21.109 9.639 1.00 23.91 A ATOM 432 CD PRO A 125 61.806 22.399 9.725 1.00 24.52 A ATOM 433 CA PRO A 125 62.737 20.736 8.239 1.00 24.57 A ATOM 434 CB PRO A 125 62.147 21.914 7.464 1.00 23.69 A ATOM 435 CG PRO A 125 61.098 22.450 8.400 1.00 25.18 A ATOM 436 C PRO A 125 64.217 20.520 7.923 1.00 23.84 A ATOM 437 O PRO A 125 64.568 19.618 7.172 1.00 22.92 A ATOM 438 N TYR A 126 65.073 21.353 8.501 1.00 24.86 A ATOM 439 CA TYR A 126 66.511 21.259 8.274 1.00 28.10 A ATOM 440 CB TYR A 126 67.202 22.494 8.859 1.00 32.76 A ATOM 441 CG TYR A 126 66.802 23.766 8.146 1.00 39.46 A ATOM 442 CD1 TYR A 126 67.466 24.179 6.987 1.00 42.04 A ATOM 443 CE1 TYR A 126 67.063 25.322 6.292 1.00 43.67 A ATOM 444 CD2 TYR A 126 65.722 24.531 8.597 1.00 42.16 A ATOM 445 CE2 TYR A 126 65.309 25.673 7.909 1.00 43.70 A ATOM 446 CZ TYR A 126 65.983 26.062 6.758 1.00 44.51 A ATOM 447 OH TYR A 126 65.570 27.183 6.068 1.00 45.30 A ATOM 448 C TYR A 126 67.115 19.984 8.852 1.00 26.14 A ATOM 449 O TYR A 126 67.768 19.225 8.141 1.00 26.15 A ATOM 450 N VAL A 127 66.891 19.756 10.141 1.00 24.35 A ATOM 451 CA VAL A 127 67.396 18.568 10.819 1.00 24.93 A ATOM 452 CB VAL A 127 66.956 18.568 12.296 1.00 24.24 A ATOM 453 CG1 VAL A 127 67.444 17.316 12.997 1.00 23.36 A ATOM 454 CG2 VAL A 127 67.492 19.809 12.979 1.00 21.11 A ATOM 455 C VAL A 127 66.894 17.290 10.130 1.00 25.81 A ATOM 456 O VAL A 127 67.655 16.351 9.903 1.00 25.79 A ATOM 457 N THR A 128 65.612 17.273 9.793 1.00 25.57 A ATOM 458 CA THR A 128 64.996 16.136 9.114 1.00 26.36 A ATOM 459 CB THR A 128 63.486 16.384 8.908 1.00 25.21 A ATOM 460 OG1 THR A 128 62.827 16.390 10.181 1.00 29.29 A ATOM 461 CG2 THR A 128 62.883 15.317 8.043 1.00 25.73 A ATOM 462 C THR A 128 65.640 15.898 7.748 1.00 26.97 A ATOM 463 O THR A 128 65.929 14.760 7.366 1.00 25.68 A ATOM 464 N ARG A 129 65.854 16.980 7.012 1.00 27.23 A ATOM 465 CA ARG A 129 66.462 16.897 5.692 1.00 29.37 A ATOM 466 CB ARG A 129 66.484 18.282 5.032 1.00 32.35 A ATOM 467 CG ARG A 129 66.936 18.280 3.583 1.003 6.81 A ATOM 468 CD ARG A 129 67.208 19.693 3.064 1.00 40.45 A ATOM 469 NE ARG A 129 66.178 20.651 3.459 1.00 44.54 A ATOM 470 CZ ARG A 129 64.874 20.474 3.268 1.00 48.21 A ATOM 471 NH1 ARG A 129 64.431 19.366 2.681 1.00 50.01 A ATOM 472 NH2 ARG A 129 64.008 21.403 3.668 1.00 47.79 A ATOM 473 C ARG A 129 67.884 16.379 5.828 1.00 28.98 A ATOM 474 O ARG A 129 68.316 15.532 5.054 1.00 28.26 A ATOM 475 N GLU A 130 68.606 16.895 6.822 1.00 29.28 A ATOM 476 CA GLU A 130 69.988 16.490 7.057 1.00 30.58 A ATOM 477 CB GLU A 130 70.556 17.203 8.287 1.00 34.18 A ATOM 478 CG GLU A 130 72.078 17.220 8.344 1.00 38.81 A ATOM 479 CD GLU A 130 72.633 17.650 9.702 1.00 41.66 A ATOM 480 OE1 GLU A 130 71.946 18.408 10.427 1.00 42.36 A ATOM 481 OE2 GLU A 130 73.771 17.236 10.035 1.00 42.31 A ATOM 482 C GLU A 130 70.063 14.984 7.273 1.00 30.12 A ATOM 483 O GLU A 130 70.861 14.298 6.638 1.00 29.62 A ATOM 484 N ARG A 131 69.228 14.474 8.173 1.00 29.21 A ATOM 485 CA ARG A 131 69.215 13.046 8.458 1.00 30.93 A ATOM 486 CB ARG A 131 68.241 12.724 9.601 1.00 32.88 A ATOM 487 CG ARG A 131 68.035 11.223 9.795 1.00 36.48 A ATOM 488 CD ARG A 131 67.069 10.885 10.922 1.00 41.14 A ATOM 489 NE ARG A 131 66.859 9.440 11.012 1.00 45.98 A ATOM 490 CZ ARG A 131 66.167 8.833 11.974 1.00 48.77 A ATOM 491 NH1 ARG A 131 65.605 9.546 12.946 1.00 48.39 A ATOM 492 NH2 ARG A 131 66.045 7.509 11.968 1.00 48.16 A ATOM 493 C ARG A 131 68.836 12.226 7.224 1.00 29.97 A ATOM 494 O ARG A 131 69.398 11.157 6.986 1.00 28.24 A ATOM 495 N ASP A 132 67.889 12.725 6.437 1.00 28.56 A ATOM 496 CA ASP A 132 67.460 11.996 5.251 1.00 29.18 A ATOM 497 CB ASP A 132 66.160 12.583 4.710 1.00 31.39 A ATOM 498 CG ASP A 132 65.005 12.409 5.682 1.00 38.76 A ATOM 499 OD1 ASP A 132 64.892 11.319 6.283 1.00 40.09 A ATOM 500 OD2 ASP A 132 64.206 13.355 5.846 1.00 44.19 A ATOM 501 C ASP A 132 68.510 11.936 4.150 1.00 27.67 A ATOM 502 O ASP A 132 68.688 10.896 3.522 1.00 27.56 A ATOM 503 N VAL A 133 69.200 13.044 3.909 1.00 26.09 A ATOM 504 CA VAL A 133 70.232 13.063 2.886 1.00 25.09 A ATOM 505 CB VAL A 133 70.859 14.459 2.742 1.00 25.26 A ATOM 506 CG1 VAL A 133 72.157 14.369 1.961 1.00 24.32 A ATOM 507 CG2 VAL A 133 69.890 15.390 2.029 1.00 24.76 A ATOM 508 C VAL A 133 71.320 12.076 3.266 1.00 25.33 A ATOM 509 O VAL A 133 71.742 11.270 2.445 1.00 23.59 A ATOM 510 N MET A 134 71.764 12.138 4.520 1.00 26.01 A ATOM 511 CA MET A 134 72.812 11.243 4.995 1.00 27.63 A ATOM 512 CB MET A 134 73.210 11.576 6.436 1.00 25.11 A ATOM 513 CG MET A 134 74.056 12.834 6.539 1.00 27.52 A ATOM 514 SD MET A 134 74.875 13.035 8.132 1.00 28.28 A ATOM 515 CE MET A 134 73.545 13.741 9.104 1.00 28.66 A ATOM 516 C MET A 134 72.431 9.779 4.901 1.00 28.59 A ATOM 517 O MET A 134 73.276 8.938 4.599 1.00 31.12 A ATOM 518 N SER A 135 71.168 9.467 5.165 1.00 29.14 A ATOM 519 CA SER A 135 70.709 8.082 5.090 1.00 31.93 A ATOM 520 CB SER A 135 69.261 7.966 5.558 1.00 32.44 A ATOM 521 OG SER A 135 69.112 8.470 6.868 1.00 40.09 A ATOM 522 C SER A 135 70.786 7.557 3.668 1.00 31.36 A ATOM 523 O SER A 135 71.010 6.374 3.454 1.00 32.23 A ATOM 524 N ARG A 136 70.597 8.448 2.701 1.00 31.66 A ATOM 525 CA ARG A 136 70.602 8.075 1.293 1.00 32.53 A ATOM 526 CB ARG A 136 69.798 9.095 0.491 1.00 33.51 A ATOM 527 CG ARG A 136 68.361 9.274 0.962 1.00 38.41 A ATOM 528 CD ARG A 136 67.676 10.352 0.137 1.00 40.27 A ATOM 529 NE ARG A 136 67.850 10.090 −1.288 1.00 42.75 A ATOM 530 CZ ARG A 136 67.560 10.953 −2.253 1.00 44.58 A ATOM 531 NH1 ARG A 136 67.071 12.151 −1.950 1.00 45.74 A ATOM 532 NH2 ARG A 136 67.771 10.621 −3.522 1.00 43.43 A ATOM 533 C ARG A 136 71.985 7.946 0.670 1.00 32.09 A ATOM 534 O ARG A 136 72.113 7.513 −0.474 1.00 32.48 A ATOM 535 N LEU A 137 73.019 8.329 1.406 1.00 30.72 A ATOM 536 CA LEU A 137 74.371 8.253 0.873 1.00 30.30 A ATOM 537 CB LEU A 137 75.167 9.508 1.262 1.00 29.84 A ATOM 538 CG LEU A 137 74.541 10.843 0.831 1.00 30.25 A ATOM 539 CD1 LEU A 137 75.488 11.963 1.154 1.00 29.16 A ATOM 540 CD2 LEU A 137 74.230 10.835 −0.656 1.00 29.68 A ATOM 541 C LEU A 137 75.083 7.006 1.369 1.00 29.52 A ATOM 542 O LEU A 137 75.033 6.684 2.553 1.00 31.12 A ATOM 543 N ASP A 138 75.745 6.310 0.453 1.00 27.02 A ATOM 544 CA ASP A 138 76.467 5.087 0.773 1.00 25.70 A ATOM 545 CB ASP A 138 75.556 3.887 0.492 1.00 29.85 A ATOM 546 CG ASP A 138 76.198 2.567 0.858 1.00 33.94 A ATOM 547 OD1 ASP A 138 76.815 2.486 1.949 1.00 34.64 A ATOM 548 OD2 ASP A 138 76.074 1.610 0.058 1.00 35.28 A ATOM 549 C ASP A 138 77.699 5.062 −0.127 1.00 24.23 A ATOM 550 O ASP A 138 77.765 4.300 −1.091 1.00 24.33 A ATOM 551 N HIS A 139 78.672 5.904 0.209 1.00 20.89 A ATOM 552 CA HIS A 139 79.888 6.069 −0.577 1.00 19.30 A ATOM 553 CB HIS A 139 79.681 7.243 −1.553 1.00 17.75 A ATOM 554 CG HIS A 139 80.774 7.410 −2.564 1.00 17.45 A ATOM 555 CD2 HIS A 139 80.794 7.179 −3.897 1.00 16.63 A ATOM 556 ND1 HIS A 139 82.034 7.862 −2.235 1.00 20.01 A ATOM 557 CE1 HIS A 139 82.784 7.901 −3.322 1.00 16.89 A ATOM 558 NE2 HIS A 139 82.054 7.491 −4.344 1.00 16.94 A ATOM 559 C HIS A 139 81.066 6.347 0.352 1.00 19.25 A ATOM 560 O HIS A 139 80.914 6.990 1.388 1.00 21.17 A ATOM 561 N PRO A 140 82.265 5.881 −0.021 1.00 17.84 A ATOM 562 CD PRO A 140 82.575 5.120 −1.243 1.00 16.07 A ATOM 563 CA PRO A 140 83.467 6.079 0.789 1.00 18.04 A ATOM 564 CB PRO A 140 84.518 5.240 0.055 1.00 18.70 A ATOM 565 CG PRO A 140 84.061 5.315 −1.365 1.00 19.17 A ATOM 566 C PRO A 140 83.919 7.523 1.014 1.00 19.75 A ATOM 567 O PRO A 140 84.686 7.793 1.930 1.00 21.01 A ATOM 568 N PHE A 141 83.460 8.457 0.192 1.00 20.21 A ATOM 569 CA PHE A 141 83.869 9.837 0.389 1.00 20.05 A ATOM 570 CB PHE A 141 84.149 10.496 −0.964 1.00 20.20 A ATOM 571 CG PHE A 141 85.333 9.909 1.686 1.00 20.95 A ATOM 572 CD1 PHE A 141 86.362 9.297 −0.975 1.00 21.45 A ATOM 573 CD2 PHE A 141 85.430 9.983 −3.071 1.00 20.27 A ATOM 574 CE1 PHE A 141 87.476 8.765 −1.635 1.00 22.05 A ATOM 575 CE2 PHE A 141 86.541 9.456 −3.743 1.00 20.58 A ATOM 576 CZ PHE A 141 87.562 8.848 −3.027 1.00 20.58 A ATOM 577 C PHE A 141 82.881 10.679 1.210 1.00 18.71 A ATOM 578 O PHE A 141 83.015 11.897 1.300 1.00 19.78 A ATOM 579 N PHE A 142 81.903 10.027 1.823 1.00 18.61 A ATOM 580 CA PHE A 142 80.915 10.738 2.639 1.00 19.11 A ATOM 581 CB PHE A 142 79.543 10.709 1.966 1.00 17.36 A ATOM 582 CG PHE A 142 79.458 11.565 0.750 1.00 19.19 A ATOM 583 CD1 PHE A 142 79.258 12.936 0.863 1.00 19.44 A ATOM 584 CD2 PHE A 142 79.649 11.016 −0.511 1.00 18.39 A ATOM 585 CE1 PHE A 142 79.254 13.759 −0.268 1.00 20.66 A ATOM 586 CE2 PHE A 142 79.648 11.824 −1.644 1.00 20.80 A ATOM 587 CZ PHE A 142 79.451 13.203 −1.523 1.00 18.95 A ATOM 588 C PHE A 142 80.787 10.132 4.023 1.00 18.98 A ATOM 589 O PHE A 142 80.735 8.918 4.168 1.00 18.39 A ATOM 590 N VAL A 143 80.736 10.983 5.041 1.00 20.79 A ATOM 591 CA VAL A 143 80.578 10.499 6.401 1.00 20.94 A ATOM 592 CB VAL A 143 80.456 11.670 7.404 1.00 21.95 A ATOM 593 CG1 VAL A 143 80.081 11.145 8.783 1.00 21.30 A ATOM 594 CG2 VAL A 143 81.781 12.433 7.473 1.00 19.28 A ATOM 595 C VAL A 143 79.299 9.683 6.396 1.00 21.12 A ATOM 596 O VAL A 143 78.280 10.124 5.895 1.00 23.63 A ATOM 597 N LYS A 144 79.367 8.481 6.940 1.00 23.64 A ATOM 598 CA LYS A 144 78.221 7.582 6.990 1.00 24.47 A ATOM 599 CB LYS A 144 78.714 6.131 6.869 1.00 25.53 A ATOM 600 CG LYS A 144 77.635 5.061 6.997 1.00 32.25 A ATOM 601 CD LYS A 144 78.240 3.660 6.870 1.00 36.07 A ATOM 602 CE LYS A 144 77.187 2.563 7.033 1.00 38.50 A ATOM 603 NZ LYS A 144 77.791 1.186 7.051 1.00 41.46 A ATOM 604 C LYS A 144 77.418 7.744 8.275 1.00 22.60 A ATOM 605 O LYS A 144 77.973 8.019 9.335 1.00 23.18 A ATOM 606 N LEU A 145 76.104 7.583 8.170 1.00 21.59 A ATOM 607 CA LEU A 145 75.224 7.661 9.327 1.00 21.42 A ATOM 608 CB LEU 145 73.918 8.372 8.967 0.50 21.21 AC1 ATOM 609 CG LEU 145 72.843 8.332 10.060 0.50 21.32 AC1 ATOM 610 CD1 LEU 145 73.356 9.036 11.309 0.50 19.59 AC1 ATOM 611 CD2 LEU 145 71.569 8.994 9.559 0.50 21.45 AC1 ATOM 612 C LEU A 145 74.919 6.215 9.733 1.00 21.84 A ATOM 613 O LEU A 145 74.283 5.471 8.977 1.00 19.24 A ATOM 614 N TYR A 146 75.363 5.816 10.921 1.00 19.77 A ATOM 615 CA TYR A 146 75.143 4.444 11.368 1.00 19.92 A ATOM 616 CB TYR A 146 76.326 3.944 12.188 1.00 18.05 A ATOM 617 CG TYR A 146 77.601 3.803 11.415 1.00 17.64 A ATOM 618 CD1 TYR A 146 78.435 4.909 11.203 1.00 18.26 A ATOM 619 CE1 TYR A 146 79.638 4.782 10.516 1.00 17.33 A ATOM 620 CD2 TYR A 146 78.000 2.560 10.910 1.00 15.57 A ATOM 621 CE2 TYR A 146 79.208 2.419 10.215 1.00 17.53 A ATOM 622 CZ TYR A 146 80.022 3.535 10.026 1.00 18.78 A ATOM 623 OH TYR A 146 81.224 3.413 9.369 1.00 19.47 A ATOM 624 C TYR A 146 73.884 4.194 12.170 1.00 20.60 A ATOM 625 O TYR A 146 73.331 3.100 12.108 1.00 21.73 A ATOM 626 N PHE A 147 73.431 5.192 12.921 1.00 20.92 A ATOM 627 CA PHE A 147 72.239 5.025 13.745 1.00 22.59 A ATOM 628 CB PHE A 147 72.538 4.063 14.917 1.00 22.24 A ATOM 629 CG PHE A 147 73.708 4.488 15.770 1.00 21.88 A ATOM 630 CD1 PHE A 147 73.607 5.578 16.625 1.00 21.93 A ATOM 631 CD2 PHE A 147 74.936 3.843 15.657 1.00 21.57 A ATOM 632 CE1 PHE A 147 74.715 6.025 17.352 1.00 25.21 A ATOM 633 CE2 PHE A 147 76.051 4.279 16.377 1.00 21.30 A ATOM 634 CZ PHE A 147 75.942 5.371 17.224 1.00 24.23 A ATOM 635 C PHE A 147 71.737 6.343 14.308 1.00 23.77 A ATOM 636 O PHE A 147 72.448 7.352 14.307 1.00 22.91 A ATOM 637 N THR A 148 70.501 6.324 14.791 1.00 25.15 A ATOM 638 CA THR A 148 69.908 7.503 15.403 1.00 25.99 A ATOM 639 CB THR A 148 68.953 8.251 14.466 1.00 27.00 A ATOM 640 OG1 THR A 148 67.850 7.400 14.148 1.00 27.79 A ATOM 641 CG2 THR A 148 69.660 8.661 13.193 1.00 26.35 A ATOM 642 C THR A 148 69.080 7.055 16.580 1.00 26.23 A ATOM 643 O THR A 148 68.591 5.930 16.620 1.00 26.46 A ATOM 644 N PHE A 149 68.942 7.943 17.550 1.00 25.72 A ATOM 645 CA PHE A 149 68.133 7.662 18.706 1.00 25.10 A ATOM 646 CB PHE A 149 68.789 6.593 19.602 1.00 23.02 A ATOM 647 CG PHE A 149 70.088 7.011 20.231 1.00 22.26 A ATOM 648 CD1 PHE A 149 70.105 7.794 21.373 1.00 20.98 A ATOM 649 CD2 PHE A 149 71.302 6.587 19.694 1.00 21.51 A ATOM 650 CE1 PHE A 149 71.312 8.151 21.976 1.00 22.36 A ATOM 651 CE2 PHE A 149 72.511 6.939 20.288 1.00 21.06 A ATOM 652 CZ PHE A 149 72.519 7.722 21.430 1.00 19.46 A ATOM 653 C PHE A 149 67.931 8.974 19.427 1.00 27.05 A ATOM 654 O PHE A 149 68.565 9.974 19.096 1.00 27.03 A ATOM 655 N GLN A 150 67.024 8.984 20.391 1.00 29.18 A ATOM 656 CA GLN A 150 66.757 10.198 21.133 1.00 31.94 A ATOM 657 CB GLN A 150 65.697 11.035 20.409 1.00 32.80 A ATOM 658 CG GLN A 150 64.385 10.302 20.153 1.00 34.22 A ATOM 659 CD GLN A 150 63.340 11.169 19.459 1.00 36.88 A ATOM 660 OE1 GLN A 150 62.630 11.959 20.098 1.00 37.60 A ATOM 661 NE2 GLN A 150 63.248 11.033 18.141 1.00 35.03 A ATOM 662 C GLN A 150 66.269 9.890 22.531 1.00 32.97 A ATOM 663 O GLN A 150 65.857 8.768 22.825 1.00 33.19 A ATOM 664 N ASP A 151 66.355 10.890 23.398 1.00 34.27 A ATOM 665 CA ASP A 151 65.847 10.771 24.753 1.00 35.77 A ATOM 666 CB ASP A 151 66.957 10.933 25.796 1.00 35.66 A ATOM 667 CG ASP A 151 67.760 12.194 25.604 1.00 38.11 A ATOM 668 OD1 ASP A 151 67.172 13.216 25.195 1.00 39.31 A ATOM 669 OD2 ASP A 151 68.982 12.167 25.879 1.00 41.03 A ATOM 670 C ASP A 151 64.823 11.904 24.838 1.00 36.64 A ATOM 671 O ASP A 151 64.401 12.428 23.803 1.00 36.42 A ATOM 672 N ASP A 152 64.427 12.301 26.041 1.00 38.18 A ATOM 673 CA ASP A 152 63.427 13.357 26.171 1.00 39.81 A ATOM 674 CB ASP A 152 63.022 13.534 27.637 1.00 44.46 A ATOM 675 CG ASP A 152 62.291 12.324 28.186 1.00 50.02 A ATOM 676 OD1 ASP A 152 61.313 11.876 27.541 1.00 52.36 A ATOM 677 OD2 ASP A 152 62.689 11.822 29.263 1.00 52.75 A ATOM 678 C ASP A 152 63.822 14.709 25.594 1.00 37.45 A ATOM 679 O ASP A 152 62.988 15.408 25.026 1.00 36.81 A ATOM 680 N GLU A 153 65.091 15.077 25.708 1.00 35.46 A ATOM 681 CA GLU A 153 65.501 16.378 25.211 1.00 33.50 A ATOM 682 CB GLU A 153 66.132 17.174 26.354 1.00 36.16 A ATOM 683 CG GLU A 153 65.389 17.065 27.687 1.00 37.72 A ATOM 684 CD GLU A 153 65.657 15.753 28.402 0.00 37.23 A ATOM 685 OE1 GLU A 153 65.063 15.530 29.479 0.00 37.39 A ATOM 686 OE2 GLU A 153 66.464 14.947 27.893 0.00 37.39 A ATOM 687 C GLU A 153 66.432 16.425 23.995 1.00 31.79 A ATOM 688 O GLU A 153 66.498 17.451 23.323 1.00 30.80 A ATOM 689 N LYS A 154 67.131 15.334 23.691 1.00 30.35 A ATOM 690 CA LYS A 154 68.069 15.357 22.569 1.00 28.14 A ATOM 691 CB LYS A 154 69.505 15.358 23.099 1.00 27.32 A ATOM 692 CG LYS A 154 69.853 16.503 24.026 1.00 29.91 A ATOM 693 CD LYS A 154 71.234 16.302 24.648 1.00 30.14 A ATOM 694 CE LYS A 154 71.606 17.450 25.592 1.00 32.52 A ATOM 695 NZ LYS A 154 72.780 17.121 26.469 1.00 31.90 A ATOM 696 C LYS A 154 67.967 14.261 21.515 1.00 26.36 A ATOM 697 O LYS A 154 67.517 13.145 21.781 1.00 23.71 A ATOM 698 N LEU A 155 68.413 14.610 20.311 1.00 24.76 A ATOM 699 CA LEU A 155 68.462 13.691 19.178 1.00 23.29 A ATOM 700 CB LEU A 155 68.012 14.382 17.891 1.00 22.72 A ATOM 701 CG LEU A 155 66.588 14.916 17.739 1.00 24.25 A ATOM 702 CD1 LEU A 155 66.441 15.489 16.329 1.00 24.62 A ATOM 703 CD2 LEU A 155 65.576 13.798 17.965 1.00 23.10 A ATOM 704 C LEU A 155 69.939 13.325 19.022 1.00 21.93 A ATOM 705 O LEU A 155 70.812 14.167 19.233 1.00 20.17 A ATOM 706 N TYR A 156 70.227 12.088 18.647 1.00 19.72 A ATOM 707 CA TYR A 156 71.617 11.693 18.462 1.00 20.11 A ATOM 708 CB TYR A 156 72.061 10.703 19.540 1.00 20.01 A ATOM 709 CG TYR A 156 71.885 11.172 20.963 1.00 20.98 A ATOM 710 CD1 TYR A 156 70.619 11.313 21.520 1.00 22.18 A ATOM 711 CE1 TYR A 156 70.457 11.724 22.850 1.00 25.21 A ATOM 712 CD2 TYR A 156 72.991 11.449 21.762 1.00 21.38 A ATOM 713 CE2 TYR A 156 72.843 11.859 23.086 1.00 25.12 A ATOM 714 CZ TYR A 156 71.576 11.995 23.622 1.00 24.83 A ATOM 715 OH TYR A 156 71.431 12.410 24.923 1.00 25.97 A ATOM 716 C TYR A 156 71.792 11.033 17.108 1.00 20.02 A ATOM 717 O TYR A 156 70.959 10.231 16.704 1.00 22.19 A ATOM 718 N PHE A 157 72.860 11.385 16.399 1.00 19.17 A ATOM 719 CA PHE A 157 73.140 10.769 15.114 1.00 18.65 A ATOM 720 CB PHE A 157 73.071 11.780 13.969 1.00 21.02 A ATOM 721 CG PHE A 157 71.719 12.411 13.791 1.00 25.64 A ATOM 722 CD1 PHE A 157 70.558 11.724 14.135 1.00 27.84 A ATOM 723 CD2 PHE A 157 71.603 13.695 13.267 1.00 27.19 A ATOM 724 CE1 PHE A 157 69.301 12.310 13.964 1.00 28.87 A ATOM 725 CE2 PHE A 157 70.350 14.288 13.091 1.00 28.27 A ATOM 726 CZ PHE A 157 69.200 13.595 13.442 1.00 26.64 A ATOM 727 C PHE A 157 74.543 10.212 15.204 1.00 19.60 A ATOM 728 O PHE A 157 75.489 10.952 15.467 1.00 19.26 A ATOM 729 N GLY A 158 74.668 8.902 15.010 1.00 19.26 A ATOM 730 CA GLY A 158 75.972 8.265 15.063 1.00 18.63 A ATOM 731 C GLY A 158 76.615 8.309 13.693 1.00 16.84 A ATOM 732 O GLY A 158 76.160 7.646 12.772 1.00 15.29 A ATOM 733 N LEU A 159 77.677 9.096 13.567 1.00 18.10 A ATOM 734 CA LEU A 159 78.386 9.263 12.302 1.00 17.32 A ATOM 735 CB LEU A 159 78.502 10.753 11.984 1.00 16.80 A ATOM 736 CG LEU A 159 77.161 11.485 12.068 1.00 18.21 A ATOM 737 CD1 LEU A 159 77.376 12.992 12.058 1.00 15.34 A ATOM 738 CD2 LEU A 159 76.280 11.036 10.906 1.00 14.27 A ATOM 739 C LEU A 159 79.780 8.665 12.375 1.00 18.27 A ATOM 740 O LEU A 159 80.338 8.518 13.465 1.00 18.92 A ATOM 741 N SER A 160 80.343 8.320 11.220 1.00 16.88 A ATOM 742 CA SER A 160 81.691 7.770 11.194 1.00 19.02 A ATOM 743 CB SER A 160 82.086 7.362 9.771 1.00 20.02 A ATOM 744 OG SER A 160 81.866 8.421 8.864 1.00 25.88 A ATOM 745 C SER A 160 82.655 8.831 11.724 1.00 18.34 A ATOM 746 O SER A 160 82.413 10.032 11.588 1.00 17.84 A ATOM 747 N TYR A 161 83.743 8.384 12.335 1.00 17.11 A ATOM 748 CA TYR A 161 84.723 9.300 12.901 1.00 19.21 A ATOM 749 CB TYR A 161 85.146 8.802 14.293 1.00 19.37 A ATOM 750 CG TYR A 161 86.269 9.582 14.944 1.00 22.52 A ATOM 751 CD1 TYR A 161 86.276 10.978 14.929 1.00 21.17 A ATOM 752 CE1 TYR A 161 87.283 11.703 15.559 1.00 18.10 A ATOM 753 CD2 TYR A 161 87.313 8.923 15.612 1.00 21.92 A ATOM 754 CE2 TYR A 161 88.330 9.647 16.252 1.00 20.10 A ATOM 755 CZ TYR A 161 88.301 11.039 16.220 1.00 20.24 A ATOM 756 OH TYR A 161 89.266 11.776 16.873 1.00 20.31 A ATOM 757 C TYR A 161 85.934 9.459 11.997 1.00 20.13 A ATOM 758 O TYR A 161 86.621 8.491 11.675 1.00 21.97 A ATOM 759 N ALA A 162 86.182 10.686 11.571 1.00 19.13 A ATOM 760 CA ALA A 162 87.320 10.969 10.717 1.00 20.60 A ATOM 761 CB ALA A 162 86.907 11.919 9.592 1.00 21.18 A ATOM 762 C ALA A 162 88.375 11.617 11.604 1.00 21.36 A ATOM 763 O ALA A 162 88.391 12.835 11.752 1.00 20.74 A ATOM 764 N LYS A 163 89.237 10.787 12.195 1.00 21.80 A ATOM 765 CA LYS A 163 90.294 11.232 13.102 1.00 25.38 A ATOM 766 CB LYS A 163 91.315 10.109 13.332 1.00 30.51 A ATOM 767 CG LYS A 163 90.874 8.987 14.251 1.00 38.24 A ATOM 768 CD LYS A 163 92.000 7.970 14.456 1.00 43.14 A ATOM 769 CE LYS A 163 91.556 6.794 15.342 1.00 46.63 A ATOM 770 NZ LYS A 163 91.252 7.200 16.752 1.00 47.21 A ATOM 771 C LYS A 163 91.082 12.482 12.719 1.00 25.07 A ATOM 772 O LYS A 163 91.276 13.373 13.541 1.00 25.50 A ATOM 773 N ASN A 164 91.540 12.549 11.477 1.00 25.06 A ATOM 774 CA ASN A 164 92.363 13.668 11.054 1.00 26.04 A ATOM 775 CB ASN A 164 93.115 13.278 9.787 1.00 26.02 A ATOM 776 CG ASN A 164 94.062 12.120 10.033 1.00 29.07 A ATOM 777 OD1 ASN A 164 94.854 12.155 10.969 1.00 30.18 A ATOM 778 ND2 ASN A 164 93.979 11.089 9.207 1.00 32.14 A ATOM 779 C ASN A 164 91.725 15.040 10.915 1.00 25.35 A ATOM 780 O ASN A 164 92.416 16.021 10.640 1.00 26.51 A ATOM 781 N GLY A 165 90.419 15.122 11.116 1.00 23.92 A ATOM 782 CA GLY A 165 89.761 16.413 11.043 1.00 24.35 A ATOM 783 C GLY A 165 89.663 17.123 9.704 1.00 23.94 A ATOM 784 O GLY A 165 89.632 16.501 8.643 1.00 25.49 A ATOM 785 N GLU A 166 89.623 18.449 9.773 1.00 23.07 A ATOM 786 CA GLU A 166 89.467 19.301 8.602 1.00 23.26 A ATOM 787 CB GLU A 166 89.164 20.739 9.036 1.00 23.73 A ATOM 788 CG GLU A 166 88.271 20.875 10.257 1.00 27.31 A ATOM 789 CD GLU A 166 87.812 22.302 10.474 1.00 29.74 A ATOM 790 OE1 GLU A 166 88.586 23.221 10.130 1.00 30.87 A ATOM 791 OE2 GLU A 166 86.686 22.510 10.989 1.00 29.80 A ATOM 792 C GLU A 166 90.612 19.354 7.602 1.00 24.47 A ATOM 793 O GLU A 166 91.786 19.473 7.968 1.00 24.85 A ATOM 794 N LEU A 167 90.251 19.287 6.328 1.00 23.47 A ATOM 795 CA LEU A 167 91.228 19.393 5.262 1.00 24.00 A ATOM 796 CB LEU A 167 90.528 19.369 3.901 1.00 22.48 A ATOM 797 CG LEU A 167 91.373 19.759 2.679 1.00 23.87 A ATOM 798 CD1 LEU A 167 92.583 18.846 2.563 1.00 20.03 A ATOM 799 CD2 LEU A 167 90.516 19.680 1.418 1.00 22.08 A ATOM 800 C LEU A 167 91.943 20.732 5.448 1.00 24.82 A ATOM 801 O LEU A 167 93.138 20.858 5.165 1.00 24.59 A ATOM 802 N LEU A 168 91.206 21.731 5.927 1.00 24.43 A ATOM 803 CA LEU A 168 91.784 23.055 6.150 1.00 28.25 A ATOM 804 CB LEU A 168 90.746 24.009 6.747 1.00 27.44 A ATOM 805 CG LEU A 168 91.310 25.395 7.090 1.00 28.57 A ATOM 806 CD1 LEU A 168 91.624 26.150 5.809 1.00 28.11 A ATOM 807 CD2 LEU A 168 90.312 26.174 7.921 1.00 29.97 A ATOM 808 C LEU A 168 92.999 23.014 7.074 1.00 28.43 A ATOM 809 O LEU A 168 93.952 23.760 6.882 1.00 30.21 A ATOM 810 N LYS A 169 92.958 22.152 8.081 1.00 30.23 A ATOM 811 CA LYS A 169 94.072 22.050 9.008 1.00 33.52 A ATOM 812 CB LYS A 169 93.821 20.955 10.046 1.00 35.45 A ATOM 813 CG LYS A 169 94.972 20.784 11.033 1.00 40.43 A ATOM 814 CD LYS A 169 94.808 19.562 11.943 1.00 41.43 A ATOM 815 CE LYS A 169 95.047 18.261 11.186 1.00 42.67 A ATOM 816 NZ LYS A 169 95.057 17.068 12.096 1.00 43.84 A ATOM 817 C LYS A 169 95.329 21.718 8.228 1.00 34.58 A ATOM 818 O LYS A 169 96.377 22.333 8.421 1.00 35.58 A ATOM 819 N TYR A 170 95.219 20.739 7.339 1.00 34.55 A ATOM 820 CA TYR A 170 96.357 20.328 6.539 1.00 35.07 A ATOM 821 CB TYR A 170 96.018 19.047 5.790 1.00 35.72 A ATOM 822 CG TYR A 170 96.050 17.869 6.716 1.00 37.48 A ATOM 823 CD1 TYR A 170 97.256 17.250 7.040 1.00 39.42 A ATOM 824 CE1 TYR A 170 97.313 16.230 7.987 1.00 40.93 A ATOM 825 CD2 TYR A 170 94.895 17.435 7.355 1.00 38.83 A ATOM 826 CE2 TYR A 170 94.937 16.417 8.303 1.00 41.76 A ATOM 827 CZ TYR A 170 96.149 15.821 8.615 1.00 42.18 A ATOM 828 OH TYR A 170 96.196 14.827 9.563 1.00 45.30 A ATOM 829 C TYR A 170 96.823 21.404 5.585 1.00 35.67 A ATOM 830 O TYR A 170 97.999 21.465 5.248 1.00 35.28 A ATOM 831 N ILE A 171 95.904 22.260 5.154 1.00 36.78 A ATOM 832 CA ILE A 171 96.272 23.333 4.252 1.00 38.95 A ATOM 833 CB ILE A 171 95.032 24.048 3.682 1.00 39.15 A ATOM 834 CG2 ILE A 171 95.452 25.329 2.960 1.00 38.11 A ATOM 835 CG1 ILE A 171 94.296 23.113 2.718 1.00 37.57 A ATOM 836 CD1 ILE A 171 93.041 23.712 2.116 1.00 37.48 A ATOM 837 C ILE A 171 97.146 24.338 4.990 1.00 41.33 A ATOM 838 O ILE A 171 98.173 24.765 4.466 1.00 42.36 A ATOM 839 N ARG A 172 96.748 24.713 6.203 1.00 42.79 A ATOM 840 CA ARG A 172 97.541 25.662 6.981 1.00 44.62 A ATOM 841 CB ARG A 172 96.809 26.103 8.253 1.00 46.82 A ATOM 842 CG ARG A 172 95.492 26.828 8.033 1.00 50.73 A ATOM 843 CD ARG A 172 95.124 27.643 9.271 1.00 53.80 A ATOM 844 NE ARG A 172 93.747 28.136 9.247 1.00 56.88 A ATOM 845 CZ ARG A 172 93.183 28.766 8.218 1.00 57.65 A ATOM 846 NH1 ARG A 172 93.873 28.989 7.104 1.00 57.71 A ATOM 847 NH2 ARG A 172 91.923 29.176 8.305 1.00 56.95 A ATOM 848 C ARG A 172 98.856 25.015 7.383 1.00 44.41 A ATOM 849 O ARG A 172 99.927 25.587 7.186 1.00 45.16 A ATOM 850 N LYS A 173 98.759 23.817 7.949 1.00 44.01 A ATOM 851 CA LYS A 173 99.923 23.069 8.398 1.00 42.99 A ATOM 852 CB LYS A 173 99.538 21.616 8.667 1.00 44.20 A ATOM 853 CG LYS A 173 100.721 20.689 8.908 1.00 45.81 A ATOM 854 CD LYS A 173 100.272 19.238 8.987 0.00 45.28 A ATOM 855 CE LYS A 173 101.457 18.296 9.120 0.00 45.43 A ATOM 856 NZ LYS A 173 101.028 16.870 9.146 0.00 45.35 A ATOM 857 C LYS A 173 101.081 23.108 7.412 1.00 43.20 A ATOM 858 O LYS A 173 102.220 23.366 7.805 1.00 43.49 A ATOM 859 N ILE A 174 100.802 22.867 6.133 1.00 41.97 A ATOM 860 CA ILE A 174 101.871 22.859 5.136 1.00 40.74 A ATOM 861 CB ILE A 174 101.874 21.536 4.336 1.00 40.61 A ATOM 862 CG2 ILE A 174 101.897 20.352 5.297 1.00 41.39 A ATOM 863 CG1 ILE A 174 100.638 21.448 3.442 1.00 40.75 A ATOM 864 CD1 ILE A 174 100.680 20.276 2.487 1.00 40.45 A ATOM 865 C ILE A 174 101.882 24.024 4.149 1.00 39.97 A ATOM 866 O ILE A 174 102.675 24.033 3.209 1.00 38.15 A ATOM 867 N GLY A 175 101.007 25.004 4.359 1.00 40.09 A ATOM 868 CA GLY A 175 100.969 26.156 3.473 1.00 39.94 A ATOM 869 C GLY A 175 100.151 25.960 2.211 1.00 39.87 A ATOM 870 O GLY A 175 99.152 26.646 2.005 1.00 40.53 A ATOM 871 N SER A 176 100.586 25.043 1.354 1.00 39.28 A ATOM 872 CA SER A 176 99.871 24.747 0.122 1.00 38.77 A ATOM 873 CB SER A 176 100.169 25.804 −0.950 1.00 39.84 A ATOM 874 OG SER A 176 101.537 25.823 −1.319 1.00 43.67 A ATOM 875 C SER A 176 100.265 23.353 −0.358 1.00 38.39 A ATOM 876 O SER A 176 101.245 22.776 0.118 1.00 39.37 A ATOM 877 N PHE A 177 99.491 22.811 −1.289 1.00 35.85 A ATOM 878 CA PHE A 177 99.732 21.472 −1.810 1.00 32.81 A ATOM 879 CB PHE A 177 98.401 20.770 −2.095 1.00 32.30 A ATOM 880 CG PHE A 177 97.645 20.344 −0.867 1.00 31.20 A ATOM 881 CD1 PHE A 177 97.806 21.005 0.348 1.00 29.02 A ATOM 882 CD2 PHE A 177 96.735 19.293 −0.939 1.00 30.11 A ATOM 883 CE1 PHE A 177 97.076 20.628 1.468 1.00 27.07 A ATOM 884 CE2 PHE A 177 95.998 18.910 0.181 1.00 29.70 A ATOM 885 CZ PHE A 177 96.170 19.580 1.385 1.00 27.57 A ATOM 886 C PHE A 177 100.535 21.485 −3.093 1.00 33.02 A ATOM 887 O PHE A 177 100.386 22.381 −3.927 1.00 30.75 A ATOM 888 N ASP A 178 101.379 20.471 −3.252 1.00 33.87 A ATOM 889 CA ASP A 178 102.184 20.329 −4.454 1.00 33.45 A ATOM 890 CB ASP A 178 103.269 19.275 −4.244 1.00 35.60 A ATOM 891 CG ASP A 178 102.693 17.932 −3.855 1.00 40.22 A ATOM 892 OD1 ASP A 178 101.840 17.412 −4.612 1.00 42.64 A ATOM 893 OD2 ASP A 178 103.079 17.398 −2.793 1.00 43.32 A ATOM 894 C ASP A 178 101.195 19.859 −5.519 1.00 32.50 A ATOM 895 O ASP A 178 99.999 19.723 −5.245 1.00 30.51 A ATOM 896 N GLU A 179 101.684 19.584 −6.720 1.00 31.46 A ATOM 897 CA GLU A 179 100.790 19.160 −7.779 1.00 32.00 A ATOM 898 CB GLU A 179 101.480 19.291 −9.138 1.00 33.70 A ATOM 899 CG GLU A 179 100.666 18.711 −10.284 1.00 38.81 A ATOM 900 CD GLU A 179 101.129 19.195 −11.646 1.00 42.71 A ATOM 901 OE1 GLU A 179 102.358 19.338 −11.844 1.00 43.96 A ATOM 902 OE2 GLU A 179 100.261 19.422 −12.523 1.00 44.44 A ATOM 903 C GLU A 179 100.189 17.766 7.635 1.00 29.96 A ATOM 904 O GLU A 179 99.023 17.564 −7.965 1.00 27.38 A ATOM 905 N THR A 180 100.959 16.803 −7.141 1.00 30.09 A ATOM 906 CA THR A 180 100.429 15.448 −7.007 1.00 29.75 A ATOM 907 CB THR A 180 101.583 14.416 −6.738 1.00 30.62 A ATOM 908 OG1 THR A 180 101.050 13.206 −6.179 1.00 30.65 A ATOM 909 CG2 THR A 180 102.615 14.991 −5.802 1.00 32.90 A ATOM 910 C THR A 180 99.331 15.372 −5.935 1.00 29.43 A ATOM 911 O THR A 180 98.312 14.710 −6.130 1.00 27.52 A ATOM 912 N CYS A 181 99.522 16.079 −4.823 1.00 29.55 A ATOM 913 CA CYS A 181 98.535 16.091 −3.745 1.00 29.27 A ATOM 914 CB CYS A 181 99.156 16.681 −2.480 1.00 31.47 A ATOM 915 SG CYS A 181 100.580 15.747 −1.838 1.00 39.84 A ATOM 916 C CYS A 181 97.271 16.879 −4.126 1.00 28.16 A ATOM 917 O CYS A 181 96.156 16.495 −3.762 1.00 26.55 A ATOM 918 N THR A 182 97.441 17.984 −4.847 1.00 25.71 A ATOM 919 CA THR A 182 96.293 18.784 −5.268 1.00 24.22 A ATOM 920 CB THR A 182 96.714 20.043 −6.066 1.00 24.45 A ATOM 921 OG1 THR A 182 97.515 20.901 −5.241 1.00 22.57 A ATOM 922 CG2 THR A 182 95.483 20.809 −6.537 1.00 23.42 A ATOM 923 C THR A 182 95.447 17.915 −6.184 1.00 24.78 A ATOM 924 O THR A 182 94.227 17.812 −6.020 1.00 23.72 A ATOM 925 N ARG A 183 96.109 17.283 −7.149 1.00 23.96 A ATOM 926 CA ARG A 183 95.422 16.419 −8.096 1.00 25.38 A ATOM 927 CB ARG A 183 96.416 15.782 −9.073 1.00 24.74 A ATOM 928 CG ARG A 183 95.740 14.821 −10.044 1.00 27.88 A ATOM 929 CD ARG A 183 96.704 14.244 −11.070 1.00 30.56 A ATOM 930 NE ARG A 183 97.260 15.300 −11.904 1.00 34.63 A ATOM 931 CZ ARG A 183 98.502 15.756 −11.802 1.00 33.50 A ATOM 932 NH1 ARG A 183 99.328 15.234 −10.903 1.00 31.79 A ATOM 933 NH2 ARG A 183 98.901 16.754 −12.579 1.00 31.24 A ATOM 934 C ARG A 183 94.648 15.318 −7.386 1.00 24.24 A ATOM 935 O ARG A 183 93.466 15.099 −7.659 1.00 24.95 A ATOM 936 N PHE A 184 95.319 14.628 −6.473 1.00 23.84 A ATOM 937 CA PHE A 184 94.689 13.541 −5.742 1.00 23.63 A ATOM 938 CB PHE A 184 95.662 12.941 −4.730 1.00 25.29 A ATOM 939 CG PHE A 184 95.086 11.787 −3.961 1.00 28.53 A ATOM 940 CD1 PHE A 184 94.958 10.531 −4.556 1.00 30.34 A ATOM 941 CD2 PHE A 184 94.620 11.964 −2.663 1.00 28.04 A ATOM 942 CE1 PHE A 184 94.370 9.465 −3.871 1.00 29.64 A ATOM 943 CE2 PHE A 184 94.030 10.908 −1.969 1.00 30.28 A ATOM 944 CZ PHE A 184 93.904 9.654 −2.576 1.00 29.09 A ATOM 945 C PHE A 184 93.431 13.977 −5.003 1.00 23.55 A ATOM 946 O PHE A 184 92.353 13.429 −5.219 1.00 24.05 A ATOM 947 N TYR A 185 93.568 14.961 −4.124 1.00 22.27 A ATOM 948 CA TYR A 185 92.429 15.408 −3.344 1.00 21.69 A ATOM 949 CB TYR A 185 92.925 16.295 −2.200 1.00 22.66 A ATOM 950 CG TYR A 185 93.539 15.447 −1.097 1.00 25.54 A ATOM 951 CD1 TYR A 185 92.738 14.614 −0.314 1.00 26.51 A ATOM 952 CE1 TYR A 185 93.290 13.738 0.620 1.00 27.53 A ATOM 953 CD2 TYR A 185 94.924 15.391 −0.908 1.00 28.66 A ATOM 954 CE2 TYR A 185 95.496 14.514 0.032 1.00 29.09 A ATOM 955 CZ TYR A 185 94.667 13.688 0.790 1.00 29.75 A ATOM 956 OH TYR A 185 95.204 12.806 1.702 1.00 29.03 A ATOM 957 C TYR A 185 91.316 16.058 −4.167 1.00 21.02 A ATOM 958 O TYR A 185 90.130 15.921 −3.851 1.00 18.76 A ATOM 959 N THR A 186 91.689 16.731 −5.244 1.00 19.87 A ATOM 960 CA THR A 186 90.690 17.337 −6.102 1.00 18.89 A ATOM 961 CB THR A 186 91.344 18.170 −7.200 1.00 19.73 A ATOM 962 OG1 THR A 186 92.115 19.218 −6.603 1.00 19.38 A ATOM 963 CG2 THR A 186 90.282 18.765 −8.125 1.00 20.16 A ATOM 964 C THR A 186 89.905 16.201 −6.753 1.00 19.05 A ATOM 965 O THR A 186 88.675 16.244 −6.855 1.00 19.38 A ATOM 966 N ALA A 187 90.627 15.180 −7.200 1.00 18.33 A ATOM 967 CA ALA A 187 89.984 14.043 −7.841 1.00 18.09 A ATOM 968 CB ALA A 187 91.024 13.035 −8.276 1.00 19.99 A ATOM 969 C ALA A 187 88.986 13.402 −6.886 1.00 18.07 A ATOM 970 O ALA A 187 87.873 13.055 −7.291 1.00 18.54 A ATOM 971 N GLU A 188 89.366 13.253 −5.617 1.00 16.56 A ATOM 972 CA GLU A 188 88.446 12.660 −4.653 1.00 16.18 A ATOM 973 CB GLU A 188 89.099 12.495 −3.280 1.00 15.52 A ATOM 974 CG GLU A 188 90.266 11.519 −3.259 1.00 20.99 A ATOM 975 CD GLU A 188 90.297 10.636 −2.013 1.00 22.64 A ATOM 976 OE1 GLU A 188 90.006 11.126 −0.899 1.00 22.95 A ATOM 977 OE2 GLU A 188 90.629 9.439 −2.149 1.00 27.37 A ATOM 978 C GLU A 188 87.189 13.508 −4.518 1.00 15.81 A ATOM 979 O GLU A 188 86.080 12.978 −4.460 1.00 15.92 A ATOM 980 N ILE A 189 87.364 14.825 −4.483 1.00 16.14 A ATOM 981 CA ILE A 189 86.235 15.733 −4.346 1.00 16.66 A ATOM 982 CB ILE A 189 86.698 17.179 −4.083 1.00 16.57 A ATOM 983 CG2 ILE A 189 85.485 18.098 −3.958 1.00 14.92 A ATOM 984 CG1 ILE A 189 87.502 17.235 −2.784 1.00 16.19 A ATOM 985 CD1 ILE A 189 88.202 18.559 −2.547 1.00 16.78 A ATOM 986 C ILE A 189 85.349 15.712 −5.580 1.00 16.29 A ATOM 987 O ILE A 189 84.123 15.667 −5.471 1.00 15.80 A ATOM 988 N VAL A 190 85.962 15.743 −6.755 1.00 16.44 A ATOM 989 CA VAL A 190 85.186 15.704 −7.985 1.00 15.98 A ATOM 990 CB VAL A 190 86.101 15.692 −9.229 1.00 17.23 A ATOM 991 CG1 VAL A 190 85.280 15.380 −10.488 1.00 16.01 A ATOM 992 CG2 VAL A 190 86.797 17.034 −9.373 1.00 13.82 A ATOM 993 C VAL A 190 84.351 14.433 −7.979 1.00 16.29 A ATOM 994 O VAL A 190 83.140 14.462 −8.194 1.00 15.64 A ATOM 995 N SER A 191 85.011 13.312 −7.723 1.00 18.94 A ATOM 996 CA SER A 191 84.337 12.015 −7.692 1.00 18.50 A ATOM 997 CB SER A 191 85.357 10.914 −7.427 1.00 19.04 A ATOM 998 OG SER A 191 84.712 9.680 −7.206 1.00 23.87 A ATOM 999 C SER A 191 83.233 11.961 −6.642 1.00 16.85 A ATOM 1000 O SER A 191 82.227 11.281 −6.818 1.00 18.11 A ATOM 1001 N ALA A 192 83.419 12.671 −5.540 1.00 17.37 A ATOM 1002 CA ALA A 192 82.395 12.687 −4.501 1.00 17.10 A ATOM 1003 CB ALA A 192 82.947 13.302 −3.222 1.00 17.08 A ATOM 1004 C ALA A 192 81.218 13.511 −5.020 1.00 18.24 A ATOM 1005 O ALA A 192 80.055 13.162 −4.798 1.00 18.91 A ATOM 1006 N LEU A 193 81.524 14.597 −5.725 1.00 16.53 A ATOM 1007 CA LEU A 193 80.483 15.453 −6.270 1.00 17.25 A ATOM 1008 CB LEU A 193 81.091 16.750 −6.826 1.00 17.70 A ATOM 1009 CG LEU A 193 81.537 17.738 −5.732 1.00 22.88 A ATOM 1010 CD1 LEU A 193 82.094 19.018 −6.348 1.00 22.13 A ATOM 1011 CD2 LEU A 193 80.345 18.057 −4.839 1.00 20.04 A ATOM 1012 C LEU A 193 79.664 14.737 −7.343 1.00 17.26 A ATOM 1013 O LEU A 193 78.442 14.893 −7.402 1.00 15.43 A ATOM 1014 N GLU A 194 80.330 13.962 −8.195 1.00 16.22 A ATOM 1015 CA GLU A 194 79.612 13.232 −9.225 1.00 19.22 A ATOM 1016 CB GLU A 194 80.564 12.405 −10.086 1.00 20.77 A ATOM 1017 CG GLU A 194 79.828 11.403 −10.978 1.00 26.27 A ATOM 1018 CD GLU A 194 80.756 10.667 −11.934 1.00 29.43 A ATOM 1019 OE1 GLU A 194 81.840 10.222 −11.489 1.00 28.21 A ATOM 1020 OE2 GLU A 194 80.392 10.532 −13.127 1.00 31.66 A ATOM 1021 C GLU A 194 78.599 12.303 −8.566 1.00 19.71 A ATOM 1022 O GLU A 194 77.466 12.159 −9.027 1.00 18.40 A ATOM 1023 N TYR A 195 79.012 11.672 −7.479 1.00 19.22 A ATOM 1024 CA TYR A 195 78.116 10.773 −6.781 1.00 19.69 A ATOM 1025 CB TYR A 195 78.867 10.041 −5.667 1.00 21.39 A ATOM 1026 CG TYR A 195 77.975 9.143 −4.847 1.00 22.55 A ATOM 1027 CD1 TYR A 195 77.596 7.881 −5.316 1.00 23.14 A ATOM 1028 CE1 TYR A 195 76.743 7.065 −4.577 1.00 22.98 A ATOM 1029 CD2 TYR A 195 77.479 9.564 −3.618 1.00 21.58 A ATOM 1030 CE2 TYR A 195 76.625 8.755 −2.872 1.00 23.50 A ATOM 1031 CZ TYR A 195 76.263 7.512 −3.358 1.00 23.18 A ATOM 1032 OH TYR A 195 75.413 6.732 −2.632 1.00 24.19 A ATOM 1033 C TYR A 195 76.939 11.546 −6.172 1.00 18.80 A ATOM 1034 O TYR A 195 75.782 11.164 −6.337 1.00 19.89 A ATOM 1035 N LEU A 196 77.242 12.629 −5.469 1.00 15.26 A ATOM 1036 CA LEU A 196 76.210 13.430 −4.813 1.00 16.52 A ATOM 1037 CB LEU A 196 76.855 14.586 −4.038 1.00 15.67 A ATOM 1038 CG LEU A 196 75.923 15.401 −3.131 1.00 19.13 A ATOM 1039 CD1 LEU A 196 75.555 14.571 −1.903 1.00 18.42 A ATOM 1040 CD2 LEU A 196 76.604 16.681 −2.689 1.00 18.50 A ATOM 1041 C LEU A 196 75.209 13.993 −5.814 1.00 18.12 A ATOM 1042 O LEU A 196 73.990 13.892 −5.637 1.00 16.25 A ATOM 1043 N HIS A 197 75.732 14.592 −6.875 1.00 17.99 A ATOM 1044 CA HIS A 197 74.873 15.171 −7.878 1.00 20.69 A ATOM 1045 CB HIS A 197 75.715 16.004 −8.832 1.00 19.71 A ATOM 1046 CG HIS A 197 76.292 17.224 −8.190 1.00 19.55 A ATOM 1047 CD2 HIS A 197 76.069 17.777 −6.973 1.00 18.32 A ATOM 1048 ND1 HIS A 197 77.172 18.063 −8.837 1.00 20.26 A ATOM 1049 CE1 HIS A 197 77.463 19.084 −8.049 1.00 20.73 A ATOM 1050 NE2 HIS A 197 76.806 18.935 −6.913 1.00 19.92 A ATOM 1051 C HIS A 197 74.091 14.093 −8.609 1.00 22.80 A ATOM 1052 O HIS A 197 72.974 14.328 −9.068 1.00 21.91 A ATOM 1053 N GLY A 198 74.672 12.903 −8.697 1.00 23.17 A ATOM 1054 CA GLY A 198 73.990 11.815 −9.366 1.00 26.22 A ATOM 1055 C GLY A 198 72.718 11.436 −8.631 1.00 27.16 A ATOM 1056 O GLY A 198 71.837 10.787 −9.185 1.00 27.89 A ATOM 1057 N LYS A 199 72.623 11.831 −7.369 1.00 27.84 A ATOM 1058 CA LYS A 199 71.429 11.532 −6.587 1.00 28.20 A ATOM 1059 CB LYS A 199 71.827 10.952 −5.227 1.00 29.35 A ATOM 1060 CG LYS A 199 72.278 9.502 −5.321 1.00 32.74 A ATOM 1061 CD LYS A 199 72.737 8.944 −3.990 1.00 38.22 A ATOM 1062 CE LYS A 199 72.600 7.424 −3.965 1.00 41.17 A ATOM 1063 NZ LYS A 199 73.173 6.779 −5.185 1.00 44.70 A ATOM 1064 C LYS A 199 70.542 12.765 −6.419 1.00 26.97 A ATOM 1065 O LYS A 199 69.678 12.807 −5.551 1.00 28.27 A ATOM 1066 N GLY A 200 70.759 13.762 −7.269 1.00 25.62 A ATOM 1067 CA GLY A 200 69.963 14.972 −7.222 1.00 24.75 A ATOM 1068 C GLY A 200 70.070 15.713 −5.908 1.00 25.82 A ATOM 1069 O GLY A 200 69.080 16.241 −5.401 1.00 26.10 A ATOM 1070 N ILE A 201 71.275 15.759 −5.353 1.00 25.31 A ATOM 1071 CA ILE A 201 71.490 16.440 −4.089 1.00 26.11 A ATOM 1072 CB ILE A 201 71.886 15.438 −2.983 1.00 27.58 A ATOM 1073 CG2 ILE A 201 72.242 16.175 −1.704 1.00 27.99 A ATOM 1074 CG1 ILE A 201 70.725 14.480 −2.719 1.00 27.89 A ATOM 1075 CD1 ILE A 201 71.068 13.366 −1.746 1.00 30.62 A ATOM 1076 C ILE A 201 72.576 17.489 −4.233 1.00 25.92 A ATOM 1077 O ILE A 201 73.599 17.269 −4.887 1.00 25.94 A ATOM 1078 N ILE A 202 72.337 18.640 −3.627 1.00 25.04 A ATOM 1079 CA ILE A 202 73.289 19.733 −3.680 1.00 26.57 A ATOM 1080 CB ILE A 202 72.640 20.990 −4.286 1.00 27.69 A ATOM 1081 CG2 ILE A 202 73.695 22.068 −4.516 1.00 30.47 A ATOM 1082 CG1 ILE A 202 71.992 20.639 −5.625 1.00 30.89 A ATOM 1083 CD1 ILE A 202 71.083 21.736 −6.178 1.00 31.79 A ATOM 1084 C ILE A 202 73.742 20.032 −2.252 1.00 26.14 A ATOM 1085 O ILE A 202 72.912 20.201 −1.351 1.00 24.75 A ATOM 1086 N HIS A 203 75.054 20.075 −2.042 1.00 25.17 A ATOM 1087 CA HIS A 203 75.585 20.362 −0.717 1.00 24.36 A ATOM 1088 CB HIS A 203 77.095 20.131 −0.677 1.00 23.06 A ATOM 1089 CG HIS A 203 77.680 20.268 0.694 1.00 24.09 A ATOM 1090 CD2 HIS A 203 77.956 21.366 1.434 1.00 22.36 A ATOM 1091 ND1 HIS A 203 77.981 19.183 1.490 1.00 23.65 A ATOM 1092 CE1 HIS A 203 78.418 19.607 2.661 1.00 23.87 A ATOM 1093 NE2 HIS A 203 78.412 20.929 2.653 1.00 25.12 A ATOM 1094 C HIS A 203 75.269 21.811 −0.330 1.00 24.71 A ATOM 1095 O HIS A 203 74.633 22.055 0.693 1.00 24.27 A ATOM 1096 N ARG A 204 75.724 22.758 −1.154 1.00 25.89 A ATOM 1097 CA ARG A 204 75.490 24.199 −0.961 1.00 25.68 A ATOM 1098 CB ARG A 204 74.033 24.471 −0.596 1.00 25.57 A ATOM 1099 CG ARG A 204 73.079 24.319 −1.751 1.00 29.26 A ATOM 1100 CD ARG A 204 71.815 25.118 −1.509 1.00 29.86 A ATOM 1101 NE ARG A 204 71.065 24.603 −0.373 1.00 33.90 A ATOM 1102 CZ ARG A 204 70.021 25.219 0.170 1.00 36.01 A ATOM 1103 NH1 ARG A 204 69.607 26.383 −0.322 1.00 37.08 A ATOM 1104 NH2 ARG A 204 69.387 24.668 1.197 1.00 34.14 A ATOM 1105 C ARG A 204 76.373 24.935 0.034 1.00 26.91 A ATOM 1106 O ARG A 204 76.210 26.144 0.243 1.00 26.29 A ATOM 1107 N ASP A 205 77.303 24.221 0.654 1.00 26.23 A ATOM 1108 CA ASP A 205 78.203 24.849 1.604 1.00 24.46 A ATOM 1109 CB ASP A 205 77.557 24.909 2.990 1.00 28.25 A ATOM 1110 CG ASP A 205 78.203 25.954 3.890 1.00 30.95 A ATOM 1111 OD1 ASP A 205 78.872 26.862 3.354 1.00 35.13 A ATOM 1112 OD2 ASP A 205 78.034 25.880 5.127 1.00 33.48 A ATOM 1113 C ASP A 205 79.483 24.039 1.631 1.00 24.22 A ATOM 1114 O ASP A 205 79.998 23.676 2.685 1.00 23.62 A ATOM 1115 N LEU A 206 79.995 23.755 0.442 1.00 23.31 A ATOM 1116 CA LEU A 206 81.206 22.978 0.321 1.00 24.19 A ATOM 1117 CB LEU A 206 81.311 22.406 −1.088 1.00 24.78 A ATOM 1118 CG LEU A 206 82.353 21.309 −1.285 1.00 25.24 A ATOM 1119 CD1 LEU A 206 82.075 20.173 −0.317 1.00 26.72 A ATOM 1120 CD2 LEU A 206 82.298 20.808 −2.720 1.00 24.32 A ATOM 1121 C LEU A 206 82.408 23.853 0.623 1.00 24.52 A ATOM 1122 O LEU A 206 82.508 24.977 0.130 1.00 24.34 A ATOM 1123 N LYS A 207 83.328 23.330 1.424 1.00 22.98 A ATOM 1124 CA LYS A 207 84.517 24.083 1.796 1.00 23.05 A ATOM 1125 CB LYS A 207 84.113 25.305 2.629 1.00 21.18 A ATOM 1126 CG LYS A 207 83.278 24.948 3.830 1.00 19.29 A ATOM 1127 CD LYS A 207 82.775 26.179 4.568 1.00 23.68 A ATOM 1128 CE LYS A 207 81.913 25.781 5.767 1.00 21.99 A ATOM 1129 NZ LYS A 207 81.580 26.910 6.686 1.00 25.14 A ATOM 1130 C LYS A 207 85.444 23.183 2.602 1.00 23.54 A ATOM 1131 O LYS A 207 85.014 22.169 3.144 1.00 26.04 A ATOM 1132 N PRO A 208 86.728 23.550 2.697 1.00 23.78 A ATOM 1133 CD PRO A 208 87.309 24.764 2.100 1.00 21.90 A ATOM 1134 CA PRO A 208 87.754 22.801 3.429 1.00 23.64 A ATOM 1135 CB PRO A 208 88.948 23.750 3.397 1.00 22.67 A ATOM 1136 CG PRO A 208 88.779 24.432 2.084 1.00 23.00 A ATOM 1137 C PRO A 208 87.393 22.390 4.859 1.00 24.47 A ATOM 1138 O PRO A 208 87.890 21.378 5.358 1.00 24.20 A ATOM 1139 N GLU A 209 86.541 23.176 5.514 1.00 25.33 A ATOM 1140 CA GLU A 209 86.132 22.903 6.894 1.00 26.78 A ATOM 1141 CB GLU A 209 85.641 24.190 7.570 1.00 27.82 A ATOM 1142 CG GLU A 209 86.616 25.359 7.479 1.00 34.76 A ATOM 1143 CD GLU A 209 86.459 26.183 6.199 1.00 39.84 A ATOM 1144 OE1 GLU A 209 86.575 25.628 5.079 1.00 38.56 A ATOM 1145 OE2 GLU A 209 86.219 27.405 6.322 1.00 44.97 A ATOM 1146 C GLU A 209 85.039 21.840 6.972 1.00 26.70 A ATOM 1147 O GLU A 209 84.786 21.269 8.035 1.00 29.78 A ATOM 1148 N ASN A 210 84.395 21.583 5.841 1.00 24.55 A ATOM 1149 CA ASN A 210 83.339 20.587 5.751 1.00 24.33 A ATOM 1150 CB ASN A 210 82.195 21.105 4.866 1.00 27.29 A ATOM 1151 CG ASN A 210 81.225 21.998 5.622 1.00 31.63 A ATOM 1152 OD1 ASN A 210 80.280 22.539 5.040 1.00 35.25 A ATOM 1153 ND2 ASN A 210 81.449 22.155 6.923 1.00 30.78 A ATOM 1154 C ASN A 210 83.885 19.289 5.158 1.00 22.61 A ATOM 1155 O ASN A 210 83.207 18.268 5.155 1.00 19.95 A ATOM 1156 N ILE A 211 85.105 19.344 4.638 1.00 22.15 A ATOM 1157 CA ILE A 211 85.733 18.174 4.043 1.00 21.36 A ATOM 1158 CB ILE A 211 86.467 18.538 2.744 1.00 20.33 A ATOM 1159 CG2 ILE A 211 87.167 17.315 2.180 1.00 20.04 A ATOM 1160 CG1 ILE A 211 85.475 19.089 1.719 1.00 19.57 A ATOM 1161 CD1 ILE A 211 86.162 19.718 0.517 1.00 20.56 A ATOM 1162 C ILE A 211 86.733 17.629 5.048 1.00 22.45 A ATOM 1163 O ILE A 211 87.805 18.209 5.254 1.00 21.87 A ATOM 1164 N LEU A 212 86.377 16.510 5.670 1.00 21.03 A ATOM 1165 CA LEU A 212 87.228 15.910 6.685 1.00 20.43 A ATOM 1166 CB LEU A 212 86.352 15.331 7.801 1.00 19.57 A ATOM 1167 CG LEU A 212 85.270 16.281 8.347 1.00 19.01 A ATOM 1168 CD1 LEU A 212 84.543 15.613 9.494 1.00 16.54 A ATOM 1169 CD2 LEU A 212 85.903 17.592 8.817 1.00 19.58 A ATOM 1170 C LEU A 212 88.148 14.833 6.139 1.00 20.95 A ATOM 1171 O LEU A 212 88.034 14.420 4.983 1.00 20.16 A ATOM 1172 N LEU A 213 89.069 14.379 6.978 1.00 21.07 A ATOM 1173 CA LEU A 213 89.991 13.330 6.578 1.00 21.58 A ATOM 1174 CB LEU A 213 91.415 13.882 6.520 1.00 21.17 A ATOM 1175 CG LEU A 213 91.633 14.944 5.440 1.00 21.26 A ATOM 1176 CD1 LEU A 213 93.051 15.466 5.514 1.00 23.93 A ATOM 1177 CD2 LEU A 213 91.378 14.335 4.070 1.00 23.36 A ATOM 1178 C LEU A 213 89.912 12.161 7.554 1.00 22.28 A ATOM 1179 O LEU A 213 89.948 12.354 8.766 1.00 23.80 A ATOM 1180 N ASN A 214 89.786 10.949 7.025 1.00 22.96 A ATOM 1181 CA ASN A 214 89.718 9.766 7.872 1.00 22.83 A ATOM 1182 CB ASN 214 88.997 8.647 7.103 0.50 23.75 AC1 ATOM 1183 CG ASN 214 89.144 7.286 7.756 0.50 25.62 AC1 ATOM 1184 OD1 ASN 214 90.212 6.673 7.713 0.50 25.34 AC1 ATOM 1185 ND2 ASN 214 88.066 6.803 8.363 0.50 26.41 AC1 ATOM 1186 C ASN A 214 91.151 9.354 8.228 1.00 23.68 A ATOM 1187 O ASN A 214 92.112 9.934 7.716 1.00 20.85 A ATOM 1188 N GLU A 215 91.291 8.379 9.119 1.00 25.06 A ATOM 1189 CA GLU A 215 92.603 7.901 9.545 1.00 26.20 A ATOM 1190 CB GLU A 215 92.453 6.669 10.435 1.00 26.19 A ATOM 1191 CG GLU A 215 93.770 6.153 10.985 1.00 29.08 A ATOM 1192 CD GLU A 215 93.589 4.963 11.907 0.00 28.21 A ATOM 1193 OE1 GLU A 215 93.064 3.927 11.449 0.00 28.42 A ATOM 1194 OE2 GLU A 215 93.973 5.065 13.092 0.00 28.42 A ATOM 1195 C GLU A 215 93.532 7.566 8.385 1.00 26.12 A ATOM 1196 O GLU A 215 94.746 7.743 8.487 1.00 29.48 A ATOM 1197 N ASP A 216 92.976 7.070 7.287 1.00 25.52 A ATOM 1198 CA ASP A 216 93.798 6.728 6.133 1.00 25.79 A ATOM 1199 CB ASP 216 93.164 5.564 5.376 0.50 27.09 AC1 ATOM 1200 CG ASP 216 93.450 4.231 6.027 0.50 29.11 AC1 ATOM 1201 OD1 ASP 216 93.206 4.098 7.244 0.50 31.09 AC1 ATOM 1202 OD2 ASP 216 93.921 3.315 5.320 0.50 31.52 AC1 ATOM 1203 C ASP A 216 94.034 7.896 5.173 1.00 24.88 A ATOM 1204 O ASP A 216 94.586 7.719 4.094 1.00 26.27 A ATOM 1205 N MET A 217 93.615 9.087 5.578 1.00 25.04 A ATOM 1206 CA MET A 217 93.789 10.301 4.792 1.00 24.86 A ATOM 1207 CB MET A 217 95.270 10.503 4.454 1.00 28.81 A ATOM 1208 CG MET A 217 96.139 10.834 5.676 1.00 29.66 A ATOM 1209 SD MET A 217 95.577 12.323 6.551 1.00 34.79 A ATOM 1210 CE MET A 217 96.130 13.598 5.411 1.00 30.61 A ATOM 1211 C MET A 217 92.942 10.437 3.528 1.00 24.93 A ATOM 1212 O MET A 217 93.277 11.215 2.629 1.00 23.08 A ATOM 1213 N HIS A 218 91.855 9.678 3.450 1.00 21.48 A ATOM 1214 CA HIS A 218 90.947 9.799 2.319 1.00 21.72 A ATOM 1215 CB HIS A 218 90.325 8.444 1.963 1.00 21.43 A ATOM 1216 CG HIS A 218 91.225 7.578 1.138 1.00 24.55 A ATOM 1217 CD2 HIS A 218 91.951 6.478 1.458 1.00 23.50 A ATOM 1218 ND1 HIS A 218 91.522 7.860 −0.179 1.00 23.64 A ATOM 1219 CE1 HIS A 218 92.392 6.975 −0.633 1.00 21.12 A ATOM 1220 NE2 HIS A 218 92.670 6.128 0.340 1.00 22.96 A ATOM 1221 C HIS A 218 89.891 10.785 2.812 1.00 20.49 A ATOM 1222 O HIS A 218 89.683 10.911 4.018 1.00 20.60 A ATOM 1223 N ILE A 219 89.231 11.488 1.897 1.00 18.82 A ATOM 1224 CA ILE A 219 88.244 12.473 2.306 1.00 17.27 A ATOM 1225 CB ILE A 219 87.914 13.487 1.178 1.00 15.59 A ATOM 1226 CG2 ILE A 219 89.175 14.201 0.718 1.00 14.62 A ATOM 1227 CG1 ILE A 219 87.252 12.769 0.006 1.00 16.04 A ATOM 1228 CD1 ILE A 219 86.458 13.685 −0.888 1.00 15.29 A ATOM 1229 C ILE A 219 86.934 11.885 2.772 1.00 17.64 A ATOM 1230 O ILE A 219 86.564 10.774 2.402 1.00 18.93 A ATOM 1231 N GLN A 220 86.240 12.658 3.597 1.00 19.19 A ATOM 1232 CA GLN A 220 84.933 12.293 4.119 1.00 21.50 A ATOM 1233 CB GLN A 220 85.061 11.585 5.475 1.00 23.96 A ATOM 1234 CG GLN A 220 85.583 10.151 5.334 1.00 29.77 A ATOM 1235 CD GLN A 220 84.945 9.182 6.319 1.00 33.77 A ATOM 1236 OE1 GLN A 220 85.257 9.188 7.513 1.00 37.87 A ATOM 1237 NE2 GLN A 220 84.040 8.347 5.821 1.00 34.29 A ATOM 1238 C GLN A 220 84.158 13.599 4.240 1.00 21.53 A ATOM 1239 O GLN A 220 84.367 14.393 5.166 1.00 22.54 A ATOM 1240 N ILE A 221 83.284 13.833 3.270 1.00 19.63 A ATOM 1241 CA ILE A 221 82.498 15.054 3.234 1.00 19.30 A ATOM 1242 CB ILE A 221 82.055 15.366 1.785 1.00 20.41 A ATOM 1243 CG2 ILE A 221 81.237 16.639 1.738 1.00 19.39 A ATOM 1244 CG1 ILE A 221 83.290 15.524 0.900 1.00 19.44 A ATOM 1245 CD1 ILE A 221 82.977 15.802 −0.550 1.00 17.44 A ATOM 1246 C ILE A 221 81.284 14.951 4.141 1.00 18.36 A ATOM 1247 O ILE A 221 80.627 13.911 4.204 1.00 15.98 A ATOM 1248 N THR A 222 80.995 16.024 4.864 1.00 19.59 A ATOM 1249 CA THR A 222 79.844 16.008 5.753 1.00 22.76 A ATOM 1250 CB THR A 222 80.218 15.420 7.126 1.00 23.86 A ATOM 1251 OG1 THR A 222 79.019 15.145 7.863 1.00 28.20 A ATOM 1252 CG2 THR A 222 81.105 16.380 7.908 1.00 23.65 A ATOM 1253 C THR A 222 79.179 17.370 5.933 1.00 23.55 A ATOM 1254 O THR A 222 79.505 18.334 5.229 1.00 25.65 A ATOM 1255 N ASP A 223 78.248 17.427 6.881 1.00 24.38 A ATOM 1256 CA ASP A 223 77.449 18.611 7.202 1.00 25.25 A ATOM 1257 CB ASP A 223 78.303 19.865 7.422 1.00 26.12 A ATOM 1258 CG ASP A 223 77.538 20.962 8.175 1.00 29.92 A ATOM 1259 OD1 ASP A 223 76.288 20.876 8.278 1.00 31.91 A ATOM 1260 OD2 ASP A 223 78.177 21.911 8.671 1.00 32.94 A ATOM 1261 C ASP A 223 76.461 18.882 6.080 1.00 25.61 A ATOM 1262 O ASP A 223 76.693 19.744 5.227 1.00 25.81 A ATOM 1263 N PHE A 224 75.358 18.139 6.098 1.00 25.18 A ATOM 1264 CA PHE A 224 74.310 18.266 5.096 1.00 26.75 A ATOM 1265 CB PHE A 224 73.860 16.879 4.635 1.00 27.24 A ATOM 1266 CG PHE A 224 74.857 16.189 3.753 1.00 28.10 A ATOM 1267 CD1 PHE A 224 74.889 16.450 2.388 1.00 29.12 A ATOM 1268 CD2 PHE A 224 75.790 15.313 4.291 1.00 28.67 A ATOM 1269 CE1 PHE A 224 75.841 15.847 1.567 1.00 30.28 A ATOM 1270 CE2 PHE A 224 76.745 14.706 3.482 1.00 31.49 A ATOM 1271 CZ PHE A 224 76.770 14.973 2.117 1.00 30.54 A ATOM 1272 C PHE A 224 73.124 19.038 5.632 1.00 27.73 A ATOM 1273 O PHE A 224 72.005 18.895 5.140 1.00 27.84 A ATOM 1274 N GLY A 225 73.378 19.862 6.643 1.00 29.36 A ATOM 1275 CA GLY A 225 72.319 20.656 7.235 1.00 30.10 A ATOM 1276 C GLY A 225 71.825 21.741 6.297 1.00 31.32 A ATOM 1277 O GLY A 225 70.714 22.248 6.451 1.00 32.90 A ATOM 1278 N THR A 226 72.640 22.091 5.311 1.00 29.95 A ATOM 1279 CA THR A 226 72.261 23.132 4.365 1.00 32.06 A ATOM 1280 CB THR A 226 73.381 24.167 4.226 1.00 33.35 A ATOM 1281 OG1 THR A 226 74.454 23.608 3.455 1.00 35.74 A ATOM 1282 CG2 THR A 226 73.920 24.542 5.593 1.00 34.02 A ATOM 1283 C THR A 226 71.979 22.551 2.983 1.00 31.11 A ATOM 1284 O THR A 226 71.801 23.288 2.012 1.00 30.89 A ATOM 1285 N ALA A 227 71.938 21.230 2.899 1.00 30.02 A ATOM 1286 CA ALA A 227 71.714 20.566 1.624 1.00 32.20 A ATOM 1287 CB ALA A 227 71.906 19.057 1.770 1.00 29.19 A ATOM 1288 C ALA A 227 70.345 20.865 1.045 1.00 32.77 A ATOM 1289 O ALA A 227 69.431 21.269 1.761 1.00 34.17 A ATOM 1290 N ALA A 228 70.229 20.684 −0.266 1.00 33.18 A ATOM 1291 CA ALA A 228 68.980 20.902 −0.982 1.00 34.43 A ATOM 1292 CB ALA A 228 69.079 22.146 −1.861 1.00 32.03 A ATOM 1293 C ALA A 228 68.742 19.674 −1.846 1.00 35.25 A ATOM 1294 O ALA A 228 69.612 19.284 −2.622 1.00 36.70 A ATOM 1295 N VAL A 229 67.578 19.056 −1.698 1.00 36.21 A ATOM 1296 CA VAL A 229 67.246 17.876 −2.488 1.00 37.95 A ATOM 1297 CB VAL A 229 66.438 16.857 −1.674 1.00 37.37 A ATOM 1298 CG1 VAL A 229 66.192 15.609 −2.506 1.00 35.62 A ATOM 1299 CG2 VAL A 229 67.176 16.522 −0.394 1.00 36.39 A ATOM 1300 C VAL A 229 66.393 18.341 −3.649 1.00 40.15 A ATOM 1301 O VAL A 229 65.353 18.965 −3.446 1.00 39.20 A ATOM 1302 N LEU A 230 66.836 18.044 −4.865 1.00 43.75 A ATOM 1303 CA LEU A 230 66.105 18.455 −6.054 1.00 48.04 A ATOM 1304 CB LEU A 230 67.039 18.473 −7.258 1.00 48.59 A ATOM 1305 CG LEU A 230 68.123 19.552 −7.212 1.00 50.35 A ATOM 1306 CD1 LEU A 230 69.118 19.312 −8.326 1.00 50.62 A ATOM 1307 CD2 LEU A 230 67.488 20.932 −7.330 1.00 50.11 A ATOM 1308 C LEU A 230 64.905 17.569 −6.346 1.00 51.38 A ATOM 1309 O LEU A 230 64.929 16.364 −6.095 1.00 51.84 A ATOM 1310 N SER A 231 63.854 18.190 −6.872 1.00 56.03 A ATOM 1311 CA SER A 231 62.616 17.502 −7.224 1.00 60.24 A ATOM 1312 CB SER A 231 61.528 17.806 −6.186 1.00 60.77 A ATOM 1313 OG SER A 231 61.222 19.192 −6.150 1.00 61.08 A ATOM 1314 C SER A 231 62.115 17.894 −8.622 1.00 62.65 A ATOM 1315 O SER A 231 61.527 17.068 −9.326 1.00 63.42 A ATOM 1316 N PRO A 232 62.334 19.161 −9.040 1.00 64.66 A ATOM 1317 CD PRO A 232 62.903 20.298 −8.289 1.00 64.95 A ATOM 1318 CA PRO A 232 61.882 19.604 −10.367 1.00 65.69 A ATOM 1319 CB PRO A 232 62.409 21.037 −10.450 1.00 65.77 A ATOM 1320 CG PRO A 232 62.341 21.493 −9.031 1.00 65.52 A ATOM 1321 C PRO A 232 62.408 18.731 −11.505 1.00 66.28 A ATOM 1322 O PRO A 232 62.858 19.241 −12.532 1.00 66.55 A ATOM 1323 N ALA A 239 65.927 26.021 −3.995 1.00 92.57 A ATOM 1324 CA ALA A 239 67.330 26.100 −3.606 1.00 92.64 A ATOM 1325 CB ALA A 239 68.187 25.262 −4.558 1.00 92.15 A ATOM 1326 C ALA A 239 67.769 27.558 −3.640 1.00 92.34 A ATOM 1327 O ALA A 239 68.683 27.930 −4.373 1.00 92.47 A ATOM 1328 N ASN A 240 67.108 28.379 −2.833 1.00 91.92 A ATOM 1329 CA ASN A 240 67.396 29.809 −2.767 1.00 91.12 A ATOM 1330 CB ASN A 240 66.374 30.566 −3.617 1.00 92.32 A ATOM 1331 CG ASN A 240 64.947 30.084 −3.378 1.00 93.20 A ATOM 1332 OD1 ASN A 240 64.471 30.061 −2.244 1.00 93.46 A ATOM 1333 ND2 ASN A 240 64.261 29.697 −4.452 1.00 94.00 A ATOM 1334 C ASN A 240 67.334 30.332 −1.335 1.00 89.78 A ATOM 1335 O ASN A 240 67.766 31.453 −1.053 1.00 89.80 A ATOM 1336 N ALA A 241 66.787 29.515 −0.441 1.00 88.16 A ATOM 1337 CA ALA A 241 66.624 29.891 0.955 1.00 86.55 A ATOM 1338 C ALA A 241 67.901 29.893 1.792 1.00 84.55 A ATOM 1339 O ALA A 241 67.865 30.268 2.961 1.00 84.76 A ATOM 1340 CB ALA A 241 65.583 28.978 1.623 1.00 88.01 A ATOM 1341 N PHE A 242 69.028 29.494 1.216 1.00 82.28 A ATOM 1342 CA PHE A 242 70.264 29.483 1.993 1.00 79.83 A ATOM 1343 CB PHE A 242 70.718 28.046 2.282 1.00 79.60 A ATOM 1344 CG PHE A 242 71.980 27.962 3.100 1.00 79.10 A ATOM 1345 CD1 PHE A 242 72.024 28.483 4.388 1.00 79.45 A ATOM 1346 CD2 PHE A 242 73.131 27.392 2.571 1.00 79.42 A ATOM 1347 CE1 PHE A 242 73.202 28.442 5.143 1.00 79.29 A ATOM 1348 CE2 PHE A 242 74.314 27.345 3.317 1.00 80.20 A ATOM 1349 CZ PHE A 242 74.348 27.872 4.605 1.00 79.98 A ATOM 1350 C PHE A 242 71.402 30.231 1.322 1.00 77.56 A ATOM 1351 O PHE A 242 71.347 30.524 0.130 1.00 78.59 A ATOM 1352 N VAL A 243 72.440 30.529 2.098 1.00 73.76 A ATOM 1353 CA VAL A 243 73.595 31.238 1.579 1.00 70.34 A ATOM 1354 CB VAL A 243 73.864 32.515 2.405 1.00 71.71 A ATOM 1355 CG1 VAL A 243 75.087 33.238 1.85 91.00 71.29 A ATOM 1356 CG2 VAL A 243 72.638 33.425 2.376 1.00 71.41 A ATOM 1357 C VAL A 243 74.851 30.362 1.581 1.00 66.69 A ATOM 1358 O VAL A 243 75.232 29.802 0.552 1.00 66.50 A ATOM 1359 N GLY A 244 75.496 30.245 2.737 1.00 62.34 A ATOM 1360 CA GLY A 244 76.708 29.444 2.829 1.00 56.48 A ATOM 1361 C GLY A 244 77.889 30.327 3.168 1.00 52.17 A ATOM 1362 O GLY A 244 77.769 31.547 3.136 1.00 52.14 A ATOM 1363 N THR A 245 79.031 29.733 3.490 1.00 48.25 A ATOM 1364 CA THR A 245 80.201 30.530 3.838 1.00 44.49 A ATOM 1365 CB THR A 245 81.413 29.633 4.106 1.00 45.53 A ATOM 1366 OG1 THR A 245 80.994 28.514 4.899 1.00 45.14 A ATOM 1367 CG2 THR A 245 82.486 30.403 4.873 1.00 42.13 A ATOM 1368 C THR A 245 80.523 31.537 2.734 1.00 40.69 A ATOM 1369 O THR A 245 80.722 31.175 1.572 1.00 38.45 A ATOM 1370 N ALA A 246 80.570 32.804 3.127 1.00 36.53 A ATOM 1371 CA ALA A 246 80.816 33.915 2.219 1.00 34.68 A ATOM 1372 CB ALA A 246 81.106 35.186 3.023 1.00 34.13 A ATOM 1373 C ALA A 246 81.896 33.718 1.164 1.00 33.21 A ATOM 1374 O ALA A 246 81.655 33.958 −0.015 1.00 33.62 A ATOM 1375 N GLN A 247 83.082 33.281 1.567 1.00 31.02 A ATOM 1376 CA GLN A 247 84.151 33.112 0.595 1.00 31.05 A ATOM 1377 CB GLN A 247 85.476 32.814 1.310 1.00 33.25 A ATOM 1378 CG GLN A 247 85.921 33.931 2.253 1.00 37.08 A ATOM 1379 CD GLN A 247 87.378 33.831 2.665 1.00 40.56 A ATOM 1380 OE1 GLN A 247 88.272 34.328 1.972 1.00 41.24 A ATOM 1381 NE2 GLN A 247 87.626 33.180 3.794 1.00 41.86 A ATOM 1382 C GLN A 247 83.895 32.069 −0.488 1.00 28.53 A ATOM 1383 O GLN A 247 84.544 32.093 −1.527 1.00 27.93 A ATOM 1384 N TYR A 248 82.934 31.177 −0.267 1.00 28.01 A ATOM 1385 CA TYR A 248 82.643 30.115 −1.238 1.00 28.20 A ATOM 1386 CB TYR A 248 82.725 28.757 −0.532 1.00 24.94 A ATOM 1387 CG TYR A 248 84.064 28.533 0.126 1.00 23.77 A ATOM 1388 CD1 TYR A 248 85.153 28.073 −0.611 1.00 23.01 A ATOM 1389 CE1 TYR A 248 86.421 27.975 −0.039 1.00 24.66 A ATOM 1390 CD2 TYR A 248 84.270 28.879 1.464 1.00 24.01 A ATOM 1391 CE2 TYR A 248 85.535 28.785 2.050 1.00 24.49 A ATOM 1392 CZ TYR A 248 86.606 28.338 1.286 1.00 26.11 A ATOM 1393 OH TYR A 248 87.868 28.305 1.828 1.00 27.54 A ATOM 1394 C TYR A 248 81.301 30.249 −1.961 1.00 28.78 A ATOM 1395 O TYR A 248 80.939 29.405 −2.777 1.00 30.26 A ATOM 1396 N VAL A 249 80.576 31.319 −1.663 1.00 28.83 A ATOM 1397 CA VAL A 249 79.281 31.584 −2.275 1.00 28.70 A ATOM 1398 CB VAL A 249 78.625 32.803 −1.601 1.00 29.37 A ATOM 1399 CG1 VAL A 249 77.333 33.163 −2.297 1.00 30.56 A ATOM 1400 CG2 VAL A 249 78.376 32.488 −0.127 1.00 31.25 A ATOM 1401 C VAL A 249 79.404 31.837 −3.779 1.00 28.19 A ATOM 1402 O VAL A 249 80.335 32.497 −4.231 1.00 27.69 A ATOM 1403 N SER A 250 78.460 31.308 −4.549 1.00 28.16 A ATOM 1404 CA SER A 250 78.476 31.481 −5.993 1.00 29.05 A ATOM 1405 CB SER A 250 77.835 30.273 −6.691 1.00 31.08 A ATOM 1406 OG SER A 250 76.497 30.058 −6.264 1.00 31.33 A ATOM 1407 C SER A 250 77.737 32.752 −6.376 1.00 29.69 A ATOM 1408 O SER A 250 76.820 33.191 −5.685 1.00 29.14 A ATOM 1409 N PRO A 251 78.131 33.361 −7.494 1.00 29.35 A ATOM 1410 CD PRO A 251 79.147 32.917 −8.463 1.00 29.28 A ATOM 1411 CA PRO A 251 77.477 34.592 −7.934 1.00 30.27 A ATOM 1412 CB PRO A 251 78.214 34.932 −9.235 1.00 29.87 A ATOM 1413 CG PRO A 251 78.687 33.588 −9.730 1.00 30.48 A ATOM 1414 C PRO A 251 75.961 34.495 −8.114 1.00 30.86 A ATOM 1415 O PRO A 251 75.246 35.442 −7.801 1.00 33.28 A ATOM 1416 N GLU A 252 75.459 33.367 −8.602 1.00 30.19 A ATOM 1417 CA GLU A 252 74.014 33.244 −8.802 1.00 30.91 A ATOM 1418 CB GLU A 252 73.649 31.903 −9.449 1.00 30.61 A ATOM 1419 CG GLU A 252 74.162 30.682 −8.689 1.00 33.88 A ATOM 1420 CD GLU A 252 75.493 30.171 −9.219 1.00 32.82 A ATOM 1421 OE1 GLU A 252 76.277 30.987 −9.747 1.00 35.25 A ATOM 1422 OE2 GLU A 252 75.756 28.956 −9.095 1.00 32.14 A ATOM 1423 C GLU A 252 73.260 33.390 −7.494 1.00 32.09 A ATOM 1424 O GLU A 252 72.157 33.928 −7.469 1.00 32.01 A ATOM 1425 N LEU A 253 73.852 32.900 −6.408 1.00 33.87 A ATOM 1426 CA LEU A 253 73.230 32.988 −5.096 1.00 35.16 A ATOM 1427 CB LEU A 253 74.031 32.183 −4.078 1.00 37.63 A ATOM 1428 CG LEU A 253 73.371 30.937 −3.479 1.00 40.98 A ATOM 1429 CD1 LEU A 253 74.302 30.321 −2.433 1.00 42.16 A ATOM 1430 CD2 LEU A 253 72.043 31.314 −2.835 1.00 40.33 A ATOM 1431 C LEU A 253 73.148 34.445 −4.640 1.00 37.20 A ATOM 1432 O LEU A 253 72.300 34.810 −3.820 1.00 37.33 A ATOM 1433 N LEU A 254 74.036 35.276 −5.171 1.00 36.48 A ATOM 1434 CA LEU A 254 74.052 36.686 −4.816 1.00 37.76 A ATOM 1435 CB LEU A 254 75.481 37.235 −4.890 1.00 35.47 A ATOM 1436 CG LEU A 254 76.512 36.692 −3.899 1.00 32.31 A ATOM 1437 CD1 LEU A 254 77.839 37.416 −4.108 1.00 32.18 A ATOM 1438 CD2 LEU A 254 76.019 36.891 −2.474 1.00 29.68 A ATOM 1439 C LEU A 254 73.150 37.496 −5.737 1.00 39.82 A ATOM 1440 O LEU A 254 72.772 38.615 −5.409 1.00 39.15 A ATOM 1441 N THR A 255 72.805 36.919 −6.885 1.00 44.09 A ATOM 1442 CA THR A 255 71.959 37.594 −7.865 1.00 47.95 A ATOM 1443 CB THR A 255 72.591 37.544 −9.276 1.00 48.10 A ATOM 1444 OG1 THR A 255 73.924 38.072 −9.227 1.00 48.96 A ATOM 1445 CG2 THR A 255 71.768 38.376 −10.253 1.00 50.10 A ATOM 1446 C THR A 255 70.538 37.032 −7.954 1.00 49.95 A ATOM 1447 O THR A 255 69.631 37.537 −7.300 1.00 51.66 A ATOM 1448 N GLU A 256 70.344 35.994 −8.764 1.00 52.84 A ATOM 1449 CA GLU A 256 69.018 35.395 −8.939 1.00 55.77 A ATOM 1450 CB GLU A 256 69.036 34.342 −10.061 1.00 55.24 A ATOM 1451 CG GLU A 256 70.360 34.171 −10.790 0.00 55.40 A ATOM 1452 CD GLU A 256 70.699 35.348 −11.681 0.00 55.34 A ATOM 1453 OE1 GLU A 256 69.831 35.760 −12.480 0.00 55.36 A ATOM 1454 OE2 GLU A 256 71.837 35.852 −11.593 0.00 55.36 A ATOM 1455 C GLU A 256 68.451 34.743 −7.677 1.00 57.04 A ATOM 1456 O GLU A 256 67.396 34.107 −7.732 1.00 56.82 A ATOM 1457 N LYS A 257 69.137 34.911 −6.549 1.00 58.87 A ATOM 1458 CA LYS A 257 68.711 34.308 −5.286 1.00 60.38 A ATOM 1459 CB LYS A 257 67.607 35.151 −4.623 1.00 60.84 A ATOM 1460 CG LYS A 257 66.327 35.322 −5.430 0.00 60.71 A ATOM 1461 CD LYS A 257 65.352 36.261 −4.731 0.00 60.78 A ATOM 1462 CE LYS A 257 64.943 35.734 −3.363 0.00 60.77 A ATOM 1463 NZ LYS A 257 63.992 36.650 −2.674 0.00 60.78 A ATOM 1464 C LYS A 257 68.227 32.878 −5.546 1.00 61.40 A ATOM 1465 O LYS A 257 67.046 32.565 −5.389 1.00 61.84 A ATOM 1466 N SER A 258 69.160 32.020 −5.958 1.00 61.26 A ATOM 1467 CA SER A 258 68.865 30.622 −6.271 1.00 61.31 A ATOM 1468 CB SER A 258 68.105 30.548 −7.605 1.00 62.95 A ATOM 1469 OG SER A 258 68.707 31.374 −8.596 1.00 63.22 A ATOM 1470 C SER A 258 70.149 29.771 −6.334 1.00 60.39 A ATOM 1471 O SER A 258 71.257 30.312 −6.329 1.00 60.58 A ATOM 1472 N ALA A 259 70.001 28.447 −6.393 1.00 57.62 A ATOM 1473 CA ALA A 259 71.159 27.551 −6.441 1.00 54.75 A ATOM 1474 CB ALA A 259 71.670 27.289 −5.025 1.00 54.90 A ATOM 1475 C ALA A 259 70.890 26.218 −7.147 1.00 52.13 A ATOM 1476 O ALA A 259 69.759 25.726 −7.175 1.00 51.63 A ATOM 1477 N CYS A 260 71.945 25.641 −7.712 1.00 48.49 A ATOM 1478 CA CYS A 260 71.848 24.371 −8.417 1.00 44.82 A ATOM 1479 CB CYS A 260 71.499 24.596 −9.890 1.00 46.78 A ATOM 1480 SG CYS A 260 72.731 25.549 −10.821 1.00 53.48 A ATOM 1481 C CYS A 260 73.176 23.643 −8.310 1.00 41.48 A ATOM 1482 O CYS A 260 74.085 24.090 −7.612 1.00 41.05 A ATOM 1483 N LYS A 261 73.288 22.525 −9.012 1.00 37.76 A ATOM 1484 CA LYS A 261 74.503 21.729 −8.980 1.00 34.90 A ATOM 1485 CB LYS A 261 74.394 20.587 −9.990 1.00 35.93 A ATOM 1486 CG LYS A 261 73.239 19.644 −9.691 1.00 38.46 A ATOM 1487 CD LYS A 261 73.239 18.430 −10.601 1.00 39.70 A ATOM 1488 CE LYS A 261 72.117 17.474 −10.229 1.00 40.95 A ATOM 1489 NZ LYS A 261 72.076 16.269 −11.110 1.00 41.64 A ATOM 1490 C LYS A 261 75.751 22.556 −9.247 1.00 32.19 A ATOM 1491 O LYS A 261 76.780 22.366 −8.595 1.00 30.08 A ATOM 1492 N SER A 262 75.651 23.480 −10.200 1.00 30.41 A ATOM 1493 CA SER A 262 76.771 24.337 −10.556 1.00 27.88 A ATOM 1494 CB SER A 262 76.361 25.333 −11.643 1.00 29.04 A ATOM 1495 OG SER A 262 76.398 24.732 −12.921 1.00 32.20 A ATOM 1496 C SER A 262 77.325 25.095 −9.360 1.00 27.01 A ATOM 1497 O SER A 262 78.515 25.403 −9.320 1.00 27.37 A ATOM 1498 N SER A 263 76.469 25.406 −8.392 1.00 24.83 A ATOM 1499 CA SER A 263 76.924 26.115 −7.201 1.00 26.29 A ATOM 1500 CB SER A 263 75.758 26.354 −6.242 1.00 26.59 A ATOM 1501 OG SER A 263 74.830 27.254 −6.832 1.00 30.68 A ATOM 1502 C SER A 263 78.039 25.337 −6.506 1.00 25.15 A ATOM 503 O SER A 263 79.034 25.924 −6.078 1.00 25.38 A ATOM 1504 N ASP A 264 77.884 24.019 −6.396 1.00 23.51 A ATOM 1505 CA ASP A 264 78.930 23.215 −5.773 1.00 22.06 A ATOM 1506 CB ASP A 264 78.500 21.754 −5.613 1.00 23.87 A ATOM 1507 CG ASP A 264 77.378 21.577 −4.599 1.00 27.11 A ATOM 1508 OD1 ASP A 264 77.276 22.402 −3.662 1.00 25.60 A ATOM 1509 OD2 ASP A 264 76.612 20.599 4.730 1.00 26.16 A ATOM 1510 C ASP A 264 80.175 23.267 −6.642 1.00 20.62 A ATOM 1511 O ASP A 264 81.289 23.339 −6.129 1.00 20.01 A ATOM 1512 N LEU A 265 79.985 23.246 −7.959 1.00 18.87 A ATOM 1513 CA LEU A 265 81.113 23.275 −8.876 1.00 20.02 A ATOM 1514 CB LEU A 265 80.634 23.131 −10.322 1.00 19.94 A ATOM 1515 CG LEU A 265 80.037 21.763 −10.672 1.00 21.08 A ATOM 1516 CD1 LEU A 265 79.580 21.771 −12.122 1.00 22.16 A ATOM 1517 CD2 LEU A 265 81.077 20.659 −10.449 1.00 16.76 A ATOM 1518 C LEU A 265 81.910 24.552 −8.705 1.00 20.53 A ATOM 1519 O LEU A 265 83.130 24.563 −8.881 1.00 21.94 A ATOM 1520 N TRP A 266 81.221 25.633 −8.361 1.00 21.74 A ATOM 1521 CA TRP A 266 81.897 26.899 −8.138 1.00 20.89 A ATOM 1522 CB TRP A 266 80.879 28.031 −7.960 1.00 22.97 A ATOM 1523 CG TRP A 266 81.477 29.309 −7.411 1.00 24.01 A ATOM 1524 CD2 TRP A 266 81.814 30.487 −8.152 1.00 23.31 A ATOM 1525 CE2 TRP A 266 82.391 31.404 −7.243 1.00 23.27 A ATOM 1526 CE3 TRP A 266 81.689 30.858 −9.497 1.00 24.79 A ATOM 1527 CD1 TRP A 266 81.850 29.555 −6.116 1.00 24.55 A ATOM 1528 NE1 TRP A 266 82.401 30.811 −6.009 1.00 23.65 A ATOM 1529 CZ2 TRP A 266 82.839 32.663 −7.636 1.00 22.89 A ATOM 1530 CZ3 TRP A 266 82.139 32.116 −9.887 1.00 23.30 A ATOM 1531 CH2 TRP A 266 82.705 33.000 −8.959 1.00 23.32 A ATOM 1532 C TRP A 266 82.739 26.735 −6.877 1.00 20.30 A ATOM 1533 O TRP A 266 83.913 27.102 −6.853 1.00 20.60 A ATOM 1534 N ALA A 267 82.141 26.175 −5.832 1.00 18.06 A ATOM 1535 CA ALA A 267 82.868 25.966 −4.584 1.00 18.46 A ATOM 1536 CB ALA A 267 81.984 25.254 −3.561 1.00 17.96 A ATOM 1537 C ALA A 267 84.112 25.132 −4.877 1.00 18.05 A ATOM 1538 O ALA A 267 85.173 25.340 −4.287 1.00 17.35 A ATOM 1539 N LEU A 268 83.982 24.190 5.799 1.00 17.12 A ATOM 1540 CA LEU A 268 85.118 23.355 −6.157 1.00 18.45 A ATOM 1541 CB LEU A 268 84.703 22.326 −7.204 1.00 17.67 A ATOM 1542 CG LEU A 268 85.809 21.436 −7.772 1.00 16.93 A ATOM 1543 CD1 LEU A 268 86.333 20.495 −6.704 1.00 17.10 A ATOM 1544 CD2 LEU A 268 85.258 20.651 −8.953 1.00 13.46 A ATOM 1545 C LEU A 268 86.232 24.249 −6.705 1.00 19.64 A ATOM 1546 O LEU A 268 87.389 24.129 −6.306 1.00 18.99 A ATOM 1547 N GLY A 269 85.869 25.158 −7.606 1.00 19.16 A ATOM 1548 CA GLY A 269 86.854 26.057 −8.178 1.00 18.25 A ATOM 1549 C GLY A 269 87.604 26.804 −7.103 1.00 20.30 A ATOM 1550 O GLY A 269 88.825 26.960 −7.178 1.00 20.24 A ATOM 1551 N CYS A 270 86.874 27.266 −6.090 1.00 20.20 A ATOM 1552 CA CYS A 270 87.486 27.996 −4.986 1.00 20.73 A ATOM 1553 CB CYS A 270 86.418 28.523 −4.031 1.00 21.05 A ATOM 1554 SG CYS A 270 85.292 29.703 −4.752 1.00 23.98 A ATOM 1555 C CYS A 270 88.417 27.082 −4.206 1.00 20.77 A ATOM 1556 O CYS A 270 89.550 27.449 −3.878 1.00 22.00 A ATOM 1557 N ILE A 271 87.927 25.886 −3.907 1.00 19.32 A ATOM 1558 CA ILE A 271 88.704 24.921 −3.147 1.00 18.46 A ATOM 1559 CB ILE A 271 87.872 23.668 −2.861 1.00 15.71 A ATOM 1560 CG2 ILE A 271 88.722 22.607 −2.182 1.00 16.51 A ATOM 1561 CG1 ILE A 271 86.688 24.051 −1.974 1.00 14.97 A ATOM 1562 CD1 ILE A 271 85.785 22.891 −1.639 1.00 17.80 A ATOM 1563 C ILE A 271 90.001 24.546 −3.856 1.00 19.30 A ATOM 1564 O ILE A 271 91.062 24.532 −3.242 1.00 21.30 A ATOM 1565 N ILE A 272 89.915 24.253 −5.147 1.00 20.07 A ATOM 1566 CA ILE A 272 91.094 23.894 −5.906 1.00 21.50 A ATOM 1567 CB ILE A 272 90.758 23.693 −7.385 1.00 22.57 A ATOM 1568 CG2 ILE A 272 92.041 23.498 −8.184 1.00 21.91 A ATOM 1569 CG1 ILE A 272 89.818 22.495 −7.542 1.00 23.57 A ATOM 1570 CD1 ILE A 272 89.314 22.294 −8.949 1.00 24.20 A ATOM 1571 C ILE A 272 92.112 25.010 −5.794 1.00 22.90 A ATOM 1572 O ILE A 272 93.287 24.783 −5.507 1.00 21.82 A ATOM 1573 N TYR A 273 91.638 26.226 −6.028 1.00 24.81 A ATOM 1574 CA TYR A 273 92.478 27.400 −5.969 1.00 25.15 A ATOM 1575 CB TYR A 273 91.630 28.632 −6.255 1.00 26.04 A ATOM 1576 CG TYR A 273 92.385 29.931 −6.173 1.00 27.80 A ATOM 1577 CD1 TYR A 273 92.715 30.500 −4.939 1.00 27.53 A ATOM 1578 CE1 TYR A 273 93.405 31.708 −4.870 1.00 27.30 A ATOM 1579 CD2 TYR A 273 92.765 30.602 −7.333 1.00 27.17 A ATOM 1580 CE2 TYR A 273 93.448 31.804 −7.277 1.00 26.68 A ATOM 1581 CZ TYR A 273 93.766 32.355 −6.050 1.00 28.05 A ATOM 1582 OH TYR A 273 94.433 33.562 −6.018 1.00 30.80 A ATOM 1583 C TYR A 273 93.139 27.521 −4.599 1.00 26.05 A ATOM 1584 O TYR A 273 94.310 27.889 −4.489 1.00 24.45 A ATOM 1585 N GLN A 274 92.380 27.205 −3.556 1.00 25.95 A ATOM 1586 CA GLN A 274 92.896 27.299 −2.202 1.00 25.98 A ATOM 1587 CB GLN A 274 91.743 27.209 −1.199 1.00 25.56 A ATOM 1588 CG GLN A 274 92.169 27.422 0.233 1.00 25.42 A ATOM 1589 CD GLN A 274 90.990 27.571 1.161 1.00 28.69 A ATOM 1590 OE1 GLN A 274 89.838 27.506 0.732 1.00 29.84 A ATOM 1591 NE2 GLN A 274 91.267 27.774 2.445 1.00 29.83 A ATOM 1592 C GLN A 274 93.951 26.231 −1.915 1.00 25.08 A ATOM 1593 O GLN A 274 94.862 26.452 −1.120 1.00 24.38 A ATOM 1594 N LEU A 275 93.838 25.081 −2.567 1.00 24.42 A ATOM 1595 CA LEU A 275 94.813 24.006 −2.369 1.00 25.43 A ATOM 1596 CB LEU A 275 94.335 22.713 −3.035 1.00 22.95 A ATOM 1597 CG LEU A 275 93.193 21.959 −2.354 1.00 25.67 A ATOM 1598 CD1 LEU A 275 92.817 20.702 −3.154 1.00 22.16 A ATOM 1599 CD2 LEU A 275 93.633 21.580 −0.950 1.00 23.32 A ATOM 1600 C LEU A 275 96.171 24.376 −2.948 1.00 25.40 A ATOM 1601 O LEU A 275 97.212 24.071 −2.376 1.00 25.87 A ATOM 1602 N VAL A 276 96.153 25.039 −4.094 1.00 25.78 A ATOM 1603 CA VAL A 276 97.384 25.419 −4.759 1.00 26.12 A ATOM 1604 CB VAL A 276 97.170 25.522 −6.280 1.00 26.14 A ATOM 1605 CG1 VAL A 276 98.492 25.783 −6.962 1.00 24.46 A ATOM 1606 CG2 VAL A 276 96.531 24.248 −6.804 1.00 22.55 A ATOM 1607 C VAL A 276 97.990 26.735 −4.275 1.00 27.83 A ATOM 1608 O VAL A 276 99.210 26.849 −4.164 1.00 29.55 A ATOM 1609 N ALA A 277 97.148 27.723 −3.990 1.00 26.88 A ATOM 1610 CA ALA A 277 97.639 29.023 −3.549 1.00 26.50 A ATOM 1611 CB ALA A 277 96.765 30.126 −4.122 1.00 24.49 A ATOM 1612 C ALA A 277 97.740 29.175 −2.035 1.00 26.79 A ATOM 1613 O ALA A 277 98.465 30.042 −1.548 1.00 28.26 A ATOM 1614 N GLY A 278 97.020 28.343 −1.290 1.00 26.17 A ATOM 1615 CA GLY A 278 97.074 28.430 0.159 1.00 24.63 A ATOM 1616 C GLY A 278 95.971 29.272 0.780 1.00 25.52 A ATOM 1617 O GLY A 278 95.793 29.259 1.998 1.00 27.25 A ATOM 1618 N LEU A 279 95.229 29.998 −0.051 1.00 24.94 A ATOM 1619 CA LEU A 279 94.130 30.849 0.408 1.00 25.58 A ATOM 1620 CB LEU A 279 94.603 32.302 0.522 1.00 27.65 A ATOM 1621 CG LEU A 279 95.748 32.631 1.470 1.00 29.35 A ATOM 1622 CD1 LEU A 279 96.365 33.958 1.075 1.00 30.47 A ATOM 1623 CD2 LEU A 279 95.232 32.671 2.892 1.00 29.70 A ATOM 1624 C LEU A 279 92.987 30.822 −0.605 1.00 25.19 A ATOM 1625 O LEU A 279 93.201 30.525 −1.781 1.00 25.34 A ATOM 1626 N PRO A 280 91.755 31.126 −0.165 1.00 23.60 A ATOM 1627 CD PRO A 280 91.306 31.357 1.216 1.00 22.97 A ATOM 1628 CA PRO A 280 90.628 31.133 −1.103 1.00 23.81 A ATOM 1629 CB PRO A 280 89.417 31.338 −0.195 1.00 25.19 A ATOM 1630 CG PRO A 280 89.982 32.041 1.008 1.00 25.48 A ATOM 1631 C PRO A 280 90.855 32.295 −2.083 1.00 26.26 A ATOM 1632 O PRO A 280 91.632 33.207 −1.792 1.00 25.42 A ATOM 1633 N PRO A 281 90.178 32.284 −3.243 1.00 26.49 A ATOM 1634 CD PRO A 281 89.182 31.285 −3.651 1.00 27.13 A ATOM 1635 CA PRO A 281 90.307 33.316 −4.281 1.00 27.25 A ATOM 1636 CB PRO A 281 89.522 32.727 −5.463 1.00 26.75 A ATOM 1637 CG PRO A 281 89.354 31.291 −5.136 1.00 25.29 A ATOM 1638 C PRO A 281 89.817 34.724 −3.954 1.00 27.30 A ATOM 1639 O PRO A 281 90.497 35.709 −4.238 1.00 27.67 A ATOM 1640 N PHE A 282 88.623 34.817 −3.388 1.00 27.79 A ATOM 1641 CA PHE A 282 88.034 36.107 −3.066 1.00 28.37 A ATOM 1642 CB PHE A 282 86.563 36.086 −3.467 1.00 27.77 A ATOM 1643 CG PHE A 282 86.335 35.557 −4.857 1.00 29.06 A ATOM 1644 CD1 PHE A 282 86.454 36.392 −5.965 1.00 28.74 A ATOM 1645 CD2 PHE A 282 86.077 34.207 −5.063 1.00 25.80 A ATOM 1646 CE1 PHE A 282 86.324 35.887 −7.255 1.00 28.50 A ATOM 1647 CE2 PHE A 282 85.947 33.695 −6.346 1.00 26.04 A ATOM 1648 CZ PHE A 282 86.071 34.535 −7.444 1.00 28.02 A ATOM 1649 C PHE A 282 88.184 36.426 −1.589 1.00 29.95 A ATOM 1650 O PHE A 282 87.600 35.763 −0.741 1.00 32.95 A ATOM 1651 N ARG A 283 88.977 37.445 −1.285 1.00 32.36 A ATOM 1652 CA ARG A 283 89.215 37.843 0.100 1.00 33.06 A ATOM 1653 CB ARG A 283 90.622 37.432 0.520 1.00 33.69 A ATOM 1654 CG ARG A 283 90.990 36.006 0.151 1.00 36.29 A ATOM 1655 CD ARG A 283 92.341 35.635 0.727 1.00 38.81 A ATOM 1656 NE ARG A 283 93.415 36.423 0.133 1.00 41.73 A ATOM 1657 CZ ARG A 283 93.783 36.338 −1.142 1.00 44.14 A ATOM 1658 NH1 ARG A 283 93.162 35.497 −1.958 1.00 45.19 A ATOM 1659 NH2 ARG A 283 94.772 37.094 −1.604 1.00 44.57 A ATOM 1660 C ARG A 283 89.065 39.353 0.267 1.00 32.44 A ATOM 1661 O ARG A 283 89.429 40.118 −0.624 1.00 31.91 A ATOM 1662 N ALA A 284 88.527 39.777 1.406 1.00 33.21 A ATOM 1663 CA ALA A 284 88.348 41.199 1.682 1.00 32.82 A ATOM 1664 CB ALA A 284 87.265 41.777 0.782 1.00 32.40 A ATOM 1665 C ALA A 284 88.004 41.445 3.147 1.00 32.98 A ATOM 1666 O ALA A 284 87.779 40.502 3.913 1.00 32.53 A ATOM 1667 N GLY A 285 87.961 42.723 3.520 1.00 32.60 A ATOM 1668 CA GLY A 285 87.666 43.112 4.887 1.00 30.00 A ATOM 1669 C GLY A 285 86.355 42.637 5.486 1.00 29.37 A ATOM 1670 O GLY A 285 86.287 42.366 6.685 1.00 29.35 A ATOM 1671 N ASN A 286 85.302 42.547 4.685 1.00 28.99 A ATOM 1672 CA ASN A 286 84.024 42.097 5.226 1.00 29.58 A ATOM 1673 CB ASN A 286 83.238 43.281 5.801 1.00 29.54 A ATOM 1674 CG ASN A 286 82.958 44.356 4.764 1.00 29.60 A ATOM 1675 OD1 ASN A 286 82.350 44.092 3.720 1.00 26.48 A ATOM 1676 ND2 ASN A 286 83.400 45.575 5.049 1.00 25.96 A ATOM 1677 C ASN A 286 83.196 41.378 4.182 1.00 30.16 A ATOM 1678 O ASN A 286 83.551 41.357 3.004 1.00 31.70 A ATOM 1679 N GLU A 287 82.084 40.796 4.613 1.00 31.14 A ATOM 1680 CA GLU A 287 81.225 40.051 3.699 1.00 32.53 A ATOM 1681 CB GLU A 287 79.943 39.600 4.397 1.00 35.66 A ATOM 1682 CG GLU A 287 80.168 38.813 5.666 1.00 43.05 A ATOM 1683 CD GLU A 287 79.138 37.707 5.856 1.00 47.79 A ATOM 1684 OE1 GLU A 287 77.933 37.959 5.616 1.00 49.01 A ATOM 1685 OE2 GLU A 287 79.539 36.588 6.256 1.00 48.82 A ATOM 1686 C GLU A 287 80.853 40.837 2.457 1.00 30.19 A ATOM 1687 O GLU A 287 80.986 40.332 1.343 1.00 30.33 A ATOM 1688 N TYR A 288 80.385 42.066 2.653 1.00 29.13 A ATOM 1689 CA TYR A 288 79.972 42.922 1.541 1.00 27.98 A ATOM 1690 CB TYR A 288 79.573 44.320 2.034 1.00 26.59 A ATOM 1691 CG TYR A 288 79.080 45.217 0.917 1.00 26.43 A ATOM 1692 CD1 TYR A 288 77.799 45.060 0.385 1.00 28.06 A ATOM 1693 CE1 TYR A 288 77.350 45.854 −0.675 1.00 28.72 A ATOM 1694 CD2 TYR A 288 79.905 46.196 0.363 1.00 27.24 A ATOM 1695 CE2 TYR A 288 79.470 46.994 −0.697 1.00 28.55 A ATOM 1696 CZ TYR A 288 78.192 46.814 −1.211 1.00 29.91 A ATOM 1697 OH TYR A 288 77.765 47.571 −2.275 1.00 30.53 A ATOM 1698 C TYR A 288 81.057 43.068 0.487 1.00 25.84 A ATOM 1699 O TYR A 288 80.790 42.940 −0.701 1.00 27.88 A ATOM 1700 N LEU A 289 82.279 43.344 0.919 1.00 24.24 A ATOM 1701 CA LEU A 289 83.382 43.495 −0.018 1.00 26.60 A ATOM 1702 CB LEU A 289 84.662 43.919 0.713 1.00 25.15 A ATOM 1703 CG LEU A 289 85.005 45.411 0.817 1.00 27.82 A ATOM 1704 CD1 LEU A 289 83.830 46.277 0.354 1.00 27.32 A ATOM 1705 CD2 LEU A 289 85.404 45.727 2.251 1.00 25.62 A ATOM 1706 C LEU A 289 83.622 42.184 −0.736 1.00 27.45 A ATOM 1707 O LEU A 289 83.901 42.157 −1.933 1.00 30.18 A ATOM 1708 N ILE A 290 83.520 41.093 0.009 1.00 28.11 A ATOM 1709 CA ILE A 290 83.726 39.770 −0.551 1.00 28.84 A ATOM 1710 CB ILE A 290 83.565 38.710 0.545 1.00 29.67 A ATOM 1711 CG2 ILE A 290 83.450 37.331 −0.071 1.00 31.47 A ATOM 1712 CG1 ILE A 290 84.756 38.802 1.504 1.00 29.26 A ATOM 1713 CD1 ILE A 290 84.604 37.995 2.779 1.00 27.48 A ATOM 1714 C ILE A 290 82.727 39.530 −1.676 1.00 27.99 A ATOM 1715 O ILE A 290 83.090 39.110 −2.775 1.00 26.63 A ATOM 1716 N PHE A 291 81.464 39.824 −1.406 1.00 28.54 A ATOM 1717 CA PHE A 291 80.432 39.638 −2.407 1.00 27.14 A ATOM 1718 CB PHE A 291 79.066 39.945 −1.807 1.00 28.37 A ATOM 1719 CG PHE A 291 78.674 39.024 −0.688 1.00 30.37 A ATOM 1720 CD1 PHE A 291 79.283 37.778 −0.543 1.00 30.07 A ATOM 1721 CD2 PHE A 291 77.658 39.377 0.194 1.00 29.74 A ATOM 1722 CE1 PHE A 291 78.885 36.897 0.463 1.00 32.11 A ATOM 1723 CE2 PHE A 291 77.253 38.502 1.202 1.00 32.76 A ATOM 1724 CZ PHE A 291 77.867 37.259 1.336 1.00 32.01 A ATOM 1725 C PHE A 291 80.690 40.525 −3.618 1.00 27.79 A ATOM 1726 O PHE A 291 80.434 40.124 −4.755 1.00 26.52 A ATOM 1727 N GLN A 292 81.200 41.730 −3.384 1.00 27.05 A ATOM 1728 CA GLN A 292 81.478 42.613 −4.503 1.00 27.48 A ATOM 1729 CB GLN A 292 82.072 43.945 −4.037 1.00 27.80 A ATOM 1730 CG GLN A 292 81.041 44.984 −3.651 1.00 30.50 A ATOM 1731 CD GLN A 292 81.630 46.381 −3.565 1.00 31.30 A ATOM 1732 OE1 GLN A 292 82.519 46.644 −2.762 1.00 33.17 A ATOM 1733 NE2 GLN A 292 81.133 47.284 −4.399 1.00 32.86 A ATOM 1734 C GLN A 292 82.442 41.934 −5.460 1.00 26.82 A ATOM 1735 O GLN A 292 82.186 41.883 −6.664 1.00 28.03 A ATOM 1736 N LYS A 293 83.539 41.402 −4.924 1.00 24.08 A ATOM 1737 CA LYS A 293 84.542 40.739 −5.751 1.00 24.43 A ATOM 1738 CB LYS A 293 85.752 40.368 −4.901 1.00 26.19 A ATOM 1739 CG LYS A 293 86.456 41.580 −4.319 1.00 28.24 A ATOM 1740 CD LYS A 293 87.750 41.213 −3.608 1.00 30.60 A ATOM 1741 CE LYS A 293 88.555 42.468 −3.273 1.00 32.23 A ATOM 1742 NZ LYS A 293 89.849 42.170 −2.591 1.00 32.86 A ATOM 1743 C LYS A 293 84.008 39.500 −6.472 1.00 25.06 A ATOM 1744 O LYS A 293 84.350 39.236 −7.628 1.00 24.96 A ATOM 1745 N ILE A 294 83.163 38.740 −5.793 1.00 24.33 A ATOM 1746 CA ILE A 294 82.593 37.552 −6.399 1.00 24.46 A ATOM 1747 CB ILE A 294 81.725 36.800 −5.385 1.00 22.52 A ATOM 1748 CG2 ILE A 294 80.837 35.783 −6.093 1.00 23.14 A ATOM 1749 CG1 ILE A 294 82.632 36.141 −4.345 1.00 21.54 A ATOM 1750 CD1 ILE A 294 81.892 35.535 −3.175 1.00 19.38 A ATOM 1751 C ILE A 294 81.761 37.885 −7.639 1.00 27.01 A ATOM 1752 O ILE A 294 81.967 37.303 −8.704 1.00 23.93 A ATOM 1753 N ILE A 295 80.830 38.828 −7.513 1.00 29.79 A ATOM 1754 CA ILE A 295 79.983 39.168 −8.653 1.00 32.98 A ATOM 1755 CB ILE A 295 78.767 40.004 −8.228 1.00 33.96 A ATOM 1756 CG2 ILE A 295 77.980 39.246 −7.174 1.00 36.23 A ATOM 1757 CG1 ILE A 295 79.216 41.358 −7.682 1.00 35.79 A ATOM 1758 CD1 ILE A 295 78.062 42.266 −7.300 1.00 37.79 A ATOM 1759 C ILE A 295 80.729 39.898 −9.757 1.00 33.17 A ATOM 1760 O ILE A 295 80.212 40.066 −10.862 1.00 34.06 A ATOM 1761 N LYS A 296 81.946 40.333 −9.462 1.00 33.65 A ATOM 1762 CA LYS A 296 82.747 41.012 −10.468 1.00 34.81 A ATOM 1763 CB LYS A 296 83.353 42.293 −9.895 1.00 38.05 A ATOM 1764 CG LYS A 296 82.353 43.427 −9.714 1.00 40.12 A ATOM 1765 CD LYS A 296 83.070 44.736 −9.401 1.00 44.01 A ATOM 1766 CE LYS A 296 82.191 45.939 −9.731 1.00 46.66 A ATOM 1767 NZ LYS A 296 82.972 47.209 −9.833 1.00 47.40 A ATOM 1768 C LYS A 296 83.851 40.078 −10.945 1.00 34.15 A ATOM 1769 O LYS A 296 84.622 40.415 −11.847 1.00 33.48 A ATOM 1770 N LEU A 297 83.907 38.897 −10.333 1.00 33.82 A ATOM 1771 CA LEU A 297 84.904 37.890 −10.663 1.00 32.06 A ATOM 1772 CB LEU A 297 84.716 37.418 −12.110 1.00 32.43 A ATOM 1773 CG LEU A 297 85.452 36.144 −12.538 1.00 33.09 A ATOM 1774 CD1 LEU A 297 84.959 34.966 −11.697 1.00 31.88 A ATOM 1775 CD2 LEU A 297 85.206 35.875 −14.025 1.00 32.51 A ATOM 1776 C LEU A 297 86.275 38.515 −10.476 1.00 32.23 A ATOM 1777 O LEU A 297 87.180 38.321 −11.278 1.00 32.08 A ATOM 1778 N GLU A 298 86.424 39.267 −9.395 1.00 33.56 A ATOM 1779 CA GLU A 298 87.682 39.936 −9.110 1.00 35.66 A ATOM 1780 CB GLU A 298 87.405 41.274 −8.428 1.00 38.03 A ATOM 1781 CG GLU A 298 88.641 42.125 −8.236 1.00 42.97 A ATOM 1782 CD GLU A 298 88.383 43.313 −7.338 1.00 46.19 A ATOM 1783 OE1 GLU A 298 87.412 44.055 −7.602 1.00 48.41 A ATOM 1784 OE2 GLU A 298 89.153 43.504 −6.369 1.00 48.44 A ATOM 1785 C GLU A 298 88.644 39.117 −8.245 1.00 34.35 A ATOM 1786 O GLU A 298 88.508 39.065 −7.021 1.00 35.64 A ATOM 1787 N TYR A 299 89.611 38.478 −8.894 1.00 32.46 A ATOM 1788 CA TYR A 299 90.624 37.678 −8.208 1.00 30.71 A ATOM 1789 CB TYR A 299 90.031 36.367 −7.672 1.00 26.01 A ATOM 1790 CG TYR A 299 89.874 35.300 −8.730 1.00 26.77 A ATOM 1791 CD1 TYR A 299 88.871 35.390 −9.699 1.00 26.60 A ATOM 1792 CE1 TYR A 299 88.768 34.448 −10.724 1.00 26.10 A ATOM 1793 CD2 TYR A 299 90.770 34.236 −8.807 1.00 22.56 A ATOM 1794 CE2 TYR A 299 90.677 33.291 −9.822 1.00 24.59 A ATOM 1795 CZ TYR A 299 89.674 33.400 −10.781 1.00 26.34 A ATOM 1796 OH TYR A 299 89.578 32.463 −11.791 1.00 22.44 A ATOM 1797 C TYR A 299 91.720 37.374 −9.229 1.00 30.95 A ATOM 1798 O TYR A 299 91.528 37.575 −10.425 1.00 28.80 A ATOM 1799 N ASP A 300 92.865 36.891 −8.764 1.00 33.38 A ATOM 1800 CA ASP A 300 93.954 36.582 −9.680 1.00 36.47 A ATOM 1801 CB ASP A 300 94.782 37.845 −9.931 1.00 42.34 A ATOM 1802 CG ASP A 300 95.014 38.644 −8.666 1.00 46.20 A ATOM 1803 OD1 ASP A 300 95.607 38.085 −7.719 1.00 49.27 A ATOM 1804 OD2 ASP A 300 94.599 39.826 −8.615 1.00 49.25 A ATOM 1805 C ASP A 300 94.848 35.444 −9.188 1.00 35.61 A ATOM 1806 O ASP A 300 94.857 35.113 −8.002 1.00 34.48 A ATOM 1807 N PHE A 301 95.602 34.854 −10.111 1.00 35.02 A ATOM 1808 CA PHE A 301 96.477 33.737 −9.781 1.00 35.94 A ATOM 1809 CB PHE A 301 96.501 32.700 −10.909 1.00 34.28 A ATOM 1810 CG PHE A 301 95.156 32.167 −11.301 1.00 32.40 A ATOM 1811 CD1 PHE A 301 94.358 32.856 −12.205 1.00 30.50 A ATOM 1812 CD2 PHE A 301 94.708 30.947 −10.803 1.00 31.83 A ATOM 1813 CE1 PHE A 301 93.131 32.333 −12.617 1.00 31.48 A ATOM 1814 CE2 PHE A 301 93.484 30.416 −11.206 1.00 31.37 A ATOM 1815 CZ PHE A 301 92.695 31.109 −12.114 1.00 31.44 A ATOM 1816 C PHE A 301 97.916 34.134 −9.524 1.00 38.11 A ATOM 1817 O PHE A 301 98.458 35.010 −10.196 1.00 39.06 A ATOM 1818 N PRO A 302 98.559 33.498 −8.535 1.00 40.47 A ATOM 1819 CD PRO A 302 98.053 32.554 −7.524 1.00 41.16 A ATOM 1820 CA PRO A 302 99.955 33.843 −8.277 1.00 41.88 A ATOM 1821 CB PRO A 302 100.248 33.131 −6.963 1.00 42.01 A ATOM 1822 CG PRO A 302 99.328 31.947 −7.001 1.00 41.79 A ATOM 1823 C PRO A 302 100.721 33.265 −9.458 1.00 44.54 A ATOM 1824 O PRO A 302 100.263 32.305 −10.082 1.00 44.30 A ATOM 1825 N GLU A 303 101.874 33.843 −9.770 1.00 47.35 A ATOM 1826 CA GLU A 303 102.667 33.395 −10.912 1.00 50.51 A ATOM 1827 CB GLU A 303 103.859 34.337 −11.105 1.00 53.23 A ATOM 1828 CG GLU A 303 104.431 34.376 −12.520 1.00 56.85 A ATOM 1829 CD GLU A 303 103.976 35.600 −13.314 1.00 59.62 A ATOM 1830 OE1 GLU A 303 104.508 35.819 −14.424 1.00 60.43 A ATOM 1831 OE2 GLU A 303 103.088 36.341 −12.834 1.00 60.45 A ATOM 1832 C GLU A 303 103.173 31.950 −10.829 1.00 50.70 A ATOM 1833 O GLU A 303 103.692 31.423 −11.815 1.00 52.21 A ATOM 1834 N ALA A 304 103.018 31.309 −9.672 1.00 49.61 A ATOM 1835 CA ALA A 304 103.495 29.933 −9.488 1.00 49.10 A ATOM 1836 CB ALA A 304 104.077 29.779 −8.082 1.00 48.82 A ATOM 1837 C ALA A 304 102.422 28.869 −9.713 1.00 47.90 A ATOM 1838 O ALA A 304 102.703 27.666 −9.719 1.00 49.41 A ATOM 1839 N PHE A 305 101.192 29.322 −9.899 1.00 44.69 A ATOM 1840 CA PHE A 305 100.053 28.440 −10.089 1.00 40.05 A ATOM 1841 CB PHE A 305 98.809 29.301 −10.299 1.00 39.69 A ATOM 1842 CG PHE A 305 97.568 28.729 −9.697 1.00 37.21 A ATOM 1843 CD1 PHE A 305 96.824 27.775 −10.379 1.00 35.36 A ATOM 1844 CD2 PHE A 305 97.133 29.157 −8.445 1.00 37.52 A ATOM 1845 CE1 PHE A 305 95.658 27.255 −9.825 1.00 34.59 A ATOM 1846 CE2 PHE A 305 95.963 28.641 −7.880 1.00 37.01 A ATOM 1847 CZ PHE A 305 95.226 27.688 −8.575 1.00 35.13 A ATOM 1848 C PHE A 305 100.197 27.435 −11.230 1.00 37.65 A ATOM 1849 O PHE A 305 100.364 27.814 −12.389 1.00 36.24 A ATOM 1850 N PHE A 306 100.120 26.150 −10.892 1.00 35.64 A ATOM 1851 CA PHE A 306 100.219 25.081 −11.884 1.00 32.40 A ATOM 1852 CB PHE A 306 99.781 23.749 −11.268 1.00 29.92 A ATOM 1853 CG PHE A 306 100.412 23.456 −9.926 1.00 28.24 A ATOM 1854 CD1 PHE A 306 101.796 23.457 −9.770 1.00 27.43 A ATOM 1855 CD2 PHE A 306 99.617 23.173 −8.816 1.00 28.59 A ATOM 1856 CE1 PHE A 306 102.380 23.181 −8.526 1.00 29.55 A ATOM 1857 CE2 PHE A 306 100.188 22.895 −7.566 1.00 29.06 A ATOM 1858 CZ PHE A 306 101.575 22.901 −7.422 1.00 29.51 A ATOM 1859 C PHE A 306 99.296 25.452 −13.047 1.00 32.76 A ATOM 1860 O PHE A 306 98.087 25.625 −12.861 1.00 34.51 A ATOM 1861 N PRO A 307 99.856 25.587 −14.262 1.00 31.43 A ATOM 1862 CD PRO A 307 101.272 25.327 −14.569 1.00 30.74 A ATOM 1863 CA PRO A 307 99.128 25.947 −15.485 1.00 29.54 A ATOM 1864 CB PRO A 307 100.158 25.700 −16.579 1.00 29.48 A ATOM 1865 CG PRO A 307 101.437 26.032 −15.895 1.00 30.81 A ATOM 1866 C PRO A 307 97.826 25.193 −15.743 1.00 29.74 A ATOM 1867 O PRO A 307 96.795 25.804 −16.022 1.00 31.08 A ATOM 1868 N LYS A 308 97.867 23.870 −15.660 1.00 28.47 A ATOM 1869 CA LYS A 308 96.672 23.086 −15.904 1.00 27.92 A ATOM 1870 CB LYS A 308 97.044 21.619 −16.114 1.00 28.70 A ATOM 1871 CG LYS A 308 97.696 21.405 −17.460 1.00 30.04 A ATOM 1872 CD LYS A 308 98.310 20.029 −17.595 1.00 33.76 A ATOM 1873 CE LYS A 308 99.106 19.926 −18.888 1.00 33.22 A ATOM 1874 NZ LYS A 308 99.897 18.663 −18.948 1.00 36.67 A ATOM 1875 C LYS A 308 95.632 23.247 −14.800 1.00 26.85 A ATOM 1876 O LYS A 308 94.433 23.170 −15.060 1.00 25.34 A ATOM 1877 N ALA A 309 96.084 23.480 −13.574 1.00 24.70 A ATOM 1878 CA ALA A 309 95.145 23.685 −12.486 1.00 24.41 A ATOM 1879 CB ALA A 309 95.855 23.652 −11.146 1.00 22.65 A ATOM 1880 C ALA A 309 94.523 25.051 −12.712 1.00 26.56 A ATOM 1881 O ALA A 309 93.327 25.238 −12.493 1.00 28.91 A ATOM 1882 N ARG A 310 95.335 26.011 −13.149 1.00 26.94 A ATOM 1883 CA ARG A 310 94.830 27.354 −13.402 1.00 27.56 A ATOM 1884 CB ARG A 310 95.961 28.289 −13.864 1.00 28.69 A ATOM 1885 CG ARG A 310 95.438 29.584 −14.480 1.00 31.42 A ATOM 1886 CD ARG A 310 96.482 30.676 −14.634 1.00 33.72 A ATOM 1887 NE ARG A 310 95.881 31.868 −15.233 1.00 37.73 A ATOM 1888 CZ ARG A 310 96.412 33.090 −15.198 1.00 38.44 A ATOM 1889 NH1 ARG A 310 97.572 33.297 −14.588 1.00 37.72 A ATOM 1890 NH2 ARG A 310 95.775 34.108 −15.767 1.00 37.74 A ATOM 1891 C ARG A 310 93.743 27.280 −14.473 1.00 26.84 A ATOM 1892 O ARG A 310 92.678 27.880 −14.344 1.00 26.39 A ATOM 1893 N ASP A 311 94.019 26.524 −15.527 1.00 26.91 A ATOM 1894 CA ASP A 311 93.069 26.369 −16.615 1.00 28.21 A ATOM 1895 CB ASP A 311 93.682 25.504 −17.713 1.00 30.32 A ATOM 1896 CG ASP A 311 92.850 25.494 −18.972 1.00 35.68 A ATOM 1897 OD1 ASP A 311 91.894 24.691 −19.040 1.00 38.27 A ATOM 1898 OD2 ASP A 311 93.145 26.302 −19.888 1.00 37.07 A ATOM 1899 C ASP A 311 91.769 25.748 −16.108 1.00 27.22 A ATOM 1900 O ASP A 311 90.678 26.205 −16.449 1.00 29.64 A ATOM 1901 N LEU A 312 91.886 24.715 −15.285 1.00 24.32 A ATOM 1902 CA LEU A 312 90.708 24.062 −14.728 1.00 23.48 A ATOM 1903 CB LEU A 312 91.118 22.838 −13.892 1.00 21.65 A ATOM 1904 CG LEU A 312 90.067 22.228 −12.945 1.00 21.40 A ATOM 1905 CD1 LEU A 312 88.789 21.917 −13.694 1.00 16.90 A ATOM 1906 CD2 LEU A 312 90.629 20.960 −12.294 1.00 19.67 A ATOM 1907 C LEU A 312 89.899 25.039 −13.871 1.00 22.73 A ATOM 1908 O LEU A 312 88.684 25.141 −14.021 1.00 22.02 A ATOM 1909 N VAL A 313 90.574 25.754 −12.972 1.00 22.12 A ATOM 1910 CA VAL A 313 89.897 26.715 −12.108 1.00 21.16 A ATOM 1911 CB VAL A 313 90.893 27.440 −11.167 1.00 23.49 A ATOM 1912 CG1 VAL A 313 90.221 28.679 −10.534 1.00 20.45 A ATOM 1913 CG2 VAL A 313 91.369 26.487 −10.080 1.00 21.63 A ATOM 1914 C VAL A 313 89.161 27.771 −12.920 1.00 22.93 A ATOM 1915 O VAL A 313 88.051 28.168 −12.566 1.00 21.46 A ATOM 1916 N GLU A 314 89.784 28.235 −14.001 1.00 23.15 A ATOM 1917 CA GLU A 314 89.156 29.252 −14.832 1.00 25.95 A ATOM 1918 CB GLU A 314 90.127 29.762 −15.900 1.00 28.61 A ATOM 1919 CG GLU A 314 91.319 30.523 −15.350 1.00 32.73 A ATOM 1920 CD GLU A 314 92.205 31.059 −16.453 1.00 35.94 A ATOM 1921 OE1 GLU A 314 92.188 30.467 −17.554 1.00 40.67 A ATOM 1922 OE2 GLU A 314 92.923 32.059 −16.225 1.00 37.73 A ATOM 1923 C GLU A 314 87.891 28.742 −15.505 1.00 24.64 A ATOM 1924 O GLU A 314 87.030 29.528 −15.892 1.00 24.01 A ATOM 1925 N LYS A 315 87.775 27.428 −15.654 1.00 23.67 A ATOM 1926 CA LYS A 315 86.588 26.874 −16.278 1.00 23.15 A ATOM 1927 CB LYS A 315 86.937 25.594 −17.042 1.00 24.76 A ATOM 1928 CG LYS A 315 87.784 25.845 −18.299 1.00 22.90 A ATOM 1929 CD LYS A 315 88.223 24.541 −18.929 1.00 23.63 A ATOM 1930 CE LYS A 315 89.079 24.772 −20.153 1.00 23.20 A ATOM 1931 NZ LYS A 315 88.332 25.582 −21.142 1.00 29.09 A ATOM 1932 C LYS A 315 85.509 26.600 −15.244 1.00 23.08 A ATOM 1933 O LYS A 315 84.386 26.250 −15.596 1.00 23.63 A ATOM 1934 N LEU A 316 85.852 26.773 −13.969 1.00 21.74 A ATOM 1935 CA LEU A 316 84.910 26.547 −12.876 1.00 21.89 A ATOM 1936 CB LEU A 316 85.569 25.738 −11.760 1.00 20.54 A ATOM 1937 CG LEU A 316 85.841 24.269 −12.090 1.00 20.69 A ATOM 1938 CD1 LEU A 316 86.600 23.611 −10.947 1.00 17.08 A ATOM 1939 CD2 LEU A 316 84.514 23.558 −12.336 1.00 19.15 A ATOM 1940 C LEU A 316 84.404 27.860 −12.312 1.00 23.66 A ATOM 1941 O LEU A 316 83.215 28.005 −12.013 1.00 25.40 A ATOM 1942 N LEU A 317 85.310 28.816 −12.149 1.00 24.48 A ATOM 1943 CA LEU A 317 84.933 30.121 −11.637 1.00 25.52 A ATOM 1944 CB LEU A 317 86.123 30.793 −10.936 1.00 24.23 A ATOM 1945 CG LEU A 317 86.656 30.035 −9.719 1.00 21.22 A ATOM 1946 CD1 LEU A 317 87.718 30.859 −9.015 1.00 23.73 A ATOM 1947 CD2 LEU A 317 85.515 29.730 −8.773 1.00 21.36 A ATOM 1948 C LEU A 317 84.459 30.953 −12.815 1.00 26.00 A ATOM 1949 O LEU A 317 85.148 31.856 −13.286 1.00 28.02 A ATOM 1950 N VAL A 318 83.272 30.611 −13.293 1.00 27.50 A ATOM 1951 CA VAL A 318 82.643 31.286 −14.421 1.00 28.43 A ATOM 1952 CB VAL A 318 82.365 30.280 −15.558 1.00 28.13 A ATOM 1953 CG1 VAL A 318 81.624 30.953 −16.694 1.00 29.20 A ATOM 1954 CG2 VAL A 318 83.677 29.689 −16.045 1.00 27.12 A ATOM 1955 C VAL A 318 81.331 31.842 −13.896 1.00 29.21 A ATOM 1956 O VAL A 318 80.559 31.120 −13.255 1.00 30.06 A ATOM 1957 N LEU A 319 81.082 33.121 −14.150 1.00 29.94 A ATOM 1958 CA LEU A 319 79.858 33.758 −13.671 1.00 30.57 A ATOM 1959 CB LEU A 319 79.808 35.214 −14.133 1.00 32.89 A ATOM 1960 CG LEU A 319 80.908 36.115 −13.553 1.00 35.26 A ATOM 1961 CD1 LEU A 319 80.741 37.551 −14.059 1.00 34.63 A ATOM 1962 CD2 LEU A 319 80.835 36.078 −12.028 1.00 34.01 A ATOM 1963 C LEU A 319 78.598 33.029 −14.117 1.00 30.01 A ATOM 1964 O LEU A 319 77.704 32.768 −13.316 1.00 30.48 A ATOM 1965 N ASP A 320 78.527 32.695 −15.397 1.00 30.13 A ATOM 1966 CA ASP A 320 77.362 31.996 −15.919 1.00 29.97 A ATOM 1967 CB ASP A 320 77.393 31.981 −17.444 1.00 32.99 A ATOM 1968 CG ASP A 320 76.116 31.435 −18.040 1.00 36.86 A ATOM 1969 OD1 ASP A 320 75.495 30.548 −17.412 1.00 38.81 A ATOM 1970 OD2 ASP A 320 75.739 31.883 −19.142 1.00 38.26 A ATOM 1971 C ASP A 320 77.373 30.569 −15.402 1.00 28.61 A ATOM 1972 O ASP A 320 78.244 29.786 −15.758 1.00 28.87 A ATOM 1973 N ALA A 321 76.398 30.233 −14.566 1.00 28.88 A ATOM 1974 CA ALA A 321 76.311 28.897 −13.980 1.00 28.04 A ATOM 1975 CB ALA A 321 75.156 28.842 −12.990 1.00 25.11 A ATOM 1976 C ALA A 321 76.151 27.794 −15.021 1.00 27.83 A ATOM 1977 O ALA A 321 76.500 26.643 −14.773 1.00 27.26 A ATOM 1978 N THR A 322 75.632 28.150 −16.190 1.00 27.45 A ATOM 1979 CA THR A 322 75.413 27.167 −17.243 1.00 27.18 A ATOM 1980 CB THR A 322 74.294 27.615 −18.191 1.00 26.99 A ATOM 1981 OG1 THR A 322 74.739 28.753 −18.940 1.00 27.15 A ATOM 1982 CG2 THR A 322 73.045 27.997 −17.399 1.00 23.11 A ATOM 1983 C THR A 322 76.654 26.909 −18.077 1.00 28.31 A ATOM 1984 O THR A 322 76.605 26.133 −19.027 1.00 28.80 A ATOM 1985 N LYS A 323 77.769 27.546 −17.727 1.00 28.30 A ATOM 1986 CA LYS A 323 78.990 27.348 −18.491 1.00 28.51 A ATOM 1987 CB LYS A 323 79.392 28.651 −19.172 1.00 30.27 A ATOM 1988 CG LYS A 323 78.305 29.160 −20.095 1.00 35.72 A ATOM 1989 CD LYS A 323 78.839 30.081 −21.170 1.00 37.65 A ATOM 1990 CE LYS A 323 77.722 30.472 −22.131 1.00 39.59 A ATOM 1991 NZ LYS A 323 77.088 29.263 −22.733 1.00 40.41 A ATOM 1992 C LYS A 323 80.154 26.799 −17.683 1.00 28.68 A ATOM 1993 O LYS A 323 81.298 26.847 −18.119 1.00 29.54 A ATOM 1994 N ARG A 324 79.866 26.271 −16.503 1.00 27.43 A ATOM 1995 CA ARG A 324 80.921 25.709 −15.684 1.00 25.01 A ATOM 1996 CB ARG A 324 80.559 25.800 −14.205 1.00 22.81 A ATOM 1997 CG ARG A 324 80.489 27.223 −13.715 1.00 21.68 A ATOM 1998 CD ARG A 324 80.036 27.315 −12.277 1.00 20.65 A ATOM 1999 NE ARG A 324 79.655 28.689 −11.971 1.00 21.18 A ATOM 2000 CZ ARG A 324 78.645 29.029 −11.180 1.00 19.20 A ATOM 2001 NH1 ARG A 324 77.909 28.093 −10.598 1.00 19.05 A ATOM 2002 NH2 ARG A 324 78.349 30.307 −11.004 1.00 19.45 A ATOM 2003 C ARG A 324 81.161 24.264 −16.073 1.00 24.64 A ATOM 2004 O ARG A 324 80.219 23.501 −16.290 1.00 23.78 A ATOM 2005 N LEU A 325 82.433 23.902 −16.177 1.00 23.92 A ATOM 2006 CA LEU A 325 82.809 22.541 −16.526 1.00 25.53 A ATOM 2007 CB LEU A 325 84.336 22.422 −16.558 1.00 25.18 A ATOM 2008 CG LEU A 325 84.995 21.178 −17.149 1.00 25.63 A ATOM 2009 CD1 LEU A 325 84.541 20.949 −18.590 1.00 25.39 A ATOM 2010 CD2 LEU A 325 86.500 21.364 17.087 1.00 23.10 A ATOM 2011 C LEU A 325 82.224 21.610 −15.466 1.00 25.01 A ATOM 2012 O LEU A 325 82.449 21.809 −14.278 1.00 23.81 A ATOM 2013 N GLY A 326 81.450 20.616 −15.900 1.00 26.41 A ATOM 2014 CA GLY A 326 80.850 19.683 −14.964 1.00 26.13 A ATOM 2015 C GLY A 326 79.338 19.771 −14.835 1.00 29.31 A ATOM 2016 O GLY A 326 78.697 18.795 −14.444 1.00 31.67 A ATOM 2017 N CYS A 327 78.753 20.918 −15.162 1.00 29.49 A ATOM 2018 CA CYS A 327 77.308 21.073 −15.042 1.00 31.91 A ATOM 2019 CB CYS A 327 76.935 22.556 −14.982 1.00 31.78 A ATOM 2020 SG CYS A 327 77.084 23.397 −16.552 1.00 38.33 A ATOM 2021 C CYS A 327 76.539 20.385 −16.175 1.00 32.76 A ATOM 2022 O CYS A 327 77.096 20.069 −17.228 1.00 32.18 A ATOM 2023 N GLU A 328 75.248 20.175 −15.952 1.00 33.60 A ATOM 2024 CA GLU A 328 74.400 19.497 −16.921 1.00 36.82 A ATOM 2025 CB GLU A 328 72.951 19.479 −16.408 1.00 41.60 A ATOM 2026 CG GLU A 328 72.845 19.437 −14.863 1.00 48.96 A ATOM 2027 CD GLU A 328 72.000 18.279 −14.321 1.00 51.75 A ATOM 2028 OE1 GLU A 328 72.393 17.103 −14.509 1.00 52.77 A ATOM 2029 OE2 GLU A 328 70.948 18.550 −13.696 1.00 52.29 A ATOM 2030 C GLU A 328 74.466 20.120 −18.317 1.00 35.83 A ATOM 2031 O GLU A 328 74.618 19.412 −19.318 1.00 34.85 A ATOM 2032 N GLU A 329 74.370 21.443 −18.378 1.00 33.75 A ATOM 2033 CA GLU A 329 74.399 22.146 −19.650 1.00 32.37 A ATOM 2034 CB GLU A 329 74.153 23.640 −19.439 1.00 34.70 A ATOM 2035 CG GLU A 329 72.898 23.972 −18.640 1.00 38.53 A ATOM 2036 CD GLU A 329 73.017 23.589 −17.172 1.00 41.60 A ATOM 2037 OE1 GLU A 329 74.048 23.926 −16.548 1.00 44.03 A ATOM 2038 OE2 GLU A 329 72.080 22.958 −16.636 1.00 44.74 A ATOM 2039 C GLU A 329 75.711 21.947 −20.399 1.00 30.96 A ATOM 2040 O GLU A 329 75.757 22.114 −21.617 1.00 28.90 A ATOM 2041 N MET A 330 76.773 21.605 −19.673 1.00 29.20 A ATOM 2042 CA MET A 330 78.075 21.379 −20.291 1.00 27.90 A ATOM 2043 CB MET A 330 79.190 22.010 −19.455 1.00 30.57 A ATOM 2044 CG MET A 330 79.189 23.536 −19.446 1.00 32.33 A ATOM 2045 SD MET A 330 79.488 24.269 −21.070 1.00 36.55 A ATOM 2046 CE MET A 330 81.257 24.001 −21.239 1.00 35.61 A ATOM 2047 C MET A 330 78.319 19.883 −20.443 1.00 27.32 A ATOM 2048 O MET A 330 79.452 19.436 −20.606 1.00 25.82 A ATOM 2049 N GLU A 331 77.232 19.122 −20.365 1.00 25.18 A ATOM 2050 CA GLU A 331 77.246 17.677 −20.526 1.00 24.56 A ATOM 2051 CB GLU A 331 77.922 17.295 −21.848 1.00 23.55 A ATOM 2052 CG GLU A 331 77.395 18.099 −23.030 1.00 25.42 A ATOM 2053 CD GLU A 331 75.867 18.176 −23.082 1.00 28.50 A ATOM 2054 OE1 GLU A 331 75.338 19.094 −23.750 1.00 31.00 A ATOM 2055 OE2 GLU A 331 75.190 17.323 −22.467 1.00 30.18 A ATOM 2056 C GLU A 331 77.804 16.834 −19.396 1.00 24.55 A ATOM 2057 O GLU A 331 78.327 15.745 −19.629 1.00 25.02 A ATOM 2058 N GLY A 332 77.692 17.339 −18.172 1.00 22.83 A ATOM 2059 CA GLY A 332 78.098 16.564 −17.017 1.00 20.57 A ATOM 2060 C GLY A 332 79.541 16.408 −16.606 1.00 20.81 A ATOM 2061 O GLY A 332 80.430 17.167 −16.999 1.00 19.36 A ATOM 2062 N TYR A 333 79.753 15.374 −15.801 1.00 20.19 A ATOM 2063 CA TYR A 333 81.053 15.056 −15.243 1.00 20.12 A ATOM 2064 CB TYR A 333 80.860 14.127 −14.052 1.00 20.05 A ATOM 2065 CG TYR A 333 80.483 14.902 −12.828 1.00 21.40 A ATOM 2066 CD1 TYR A 333 81.464 15.367 −11.956 1.00 22.85 A ATOM 2067 CE1 TYR A 333 81.141 16.181 −10.878 1.00 22.91 A ATOM 2068 CD2 TYR A 333 79.160 15.266 −12.590 1.00 21.24 A ATOM 2069 CE2 TYR A 333 78.827 16.082 −11.518 1.00 22.71 A ATOM 2070 CZ TYR A 333 79.827 16.535 −10.670 1.00 21.44 A ATOM 2071 OH TYR A 333 79.522 17.358 −9.621 1.00 24.72 A ATOM 2072 C TYR A 333 82.076 14.484 −16.192 1.00 20.38 A ATOM 2073 O TYR A 333 83.277 14.533 −15.910 1.00 18.82 A ATOM 2074 N GLY A 334 81.610 13.942 −17.313 1.00 20.41 A ATOM 2075 CA GLY A 334 82.534 13.378 −18.280 1.00 20.48 A ATOM 2076 C GLY A 334 83.611 14.367 −18.693 1.00 20.12 A ATOM 2077 O GLY A 334 84.808 14.105 −18.539 1.00 21.13 A ATOM 2078 N PRO A 335 83.216 15.524 −19.230 1.00 19.75 A ATOM 2079 CD PRO A 335 81.872 15.899 −19.699 1.00 19.25 A ATOM 2080 CA PRO A 335 84.218 16.512 −19.644 1.00 19.66 A ATOM 2081 CB PRO A 335 83.366 17.644 −20.212 1.00 17.92 A ATOM 2082 CG PRO A 335 82.184 16.901 −20.784 1.00 19.24 A ATOM 2083 C PRO A 335 85.115 16.967 −18.495 1.00 19.62 A ATOM 2084 O PRO A 335 86.315 17.154 −18.679 1.00 21.87 A ATOM 2085 N LEU A 336 84.538 17.131 −17.307 1.00 19.91 A ATOM 2086 CA LEU A 336 85.312 17.576 −16.147 1.00 19.06 A ATOM 2087 CB LEU A 336 84.406 17.767 −14.914 1.00 18.05 A ATOM 2088 CG LEU A 336 85.073 18.119 −13.571 1.00 18.25 A ATOM 2089 CD1 LEU A 336 86.049 19.280 −13.746 1.00 15.57 A ATOM 2090 CD2 LEU A 336 84.009 18.473 −12.538 1.00 15.31 A ATOM 2091 C LEU A 336 86.424 16.594 −15.832 1.00 17.85 A ATOM 2092 O LEU A 336 87.582 16.986 −15.690 1.00 17.14 A ATOM 2093 N LYS A 337 86.075 15.317 −15.732 1.00 17.96 A ATOM 2094 CA LYS A 337 87.061 14.289 −15.438 1.00 19.15 A ATOM 2095 CB LYS A 337 86.352 12.966 −15.134 1.00 21.53 A ATOM 2096 CG LYS A 337 85.571 13.025 −13.821 1.00 25.58 A ATOM 2097 CD LYS A 337 84.484 11.956 −13.715 1.00 26.69 A ATOM 2098 CE LYS A 337 85.063 10.566 −13.571 1.00 29.78 A ATOM 2099 NZ LYS A 337 83.979 9.552 −13.368 1.00 30.74 A ATOM 2100 C LYS A 337 88.065 14.120 −16.576 1.00 21.13 A ATOM 2101 O LYS A 337 89.170 13.631 −16.362 1.00 21.11 A ATOM 2102 N ALA A 338 87.697 14.549 −17.780 1.00 21.55 A ATOM 2103 CA ALA A 338 88.600 14.426 −18.922 1.00 22.23 A ATOM 2104 CB ALA A 338 87.802 14.368 −20.221 1.00 21.66 A ATOM 2105 C ALA A 338 89.604 15.569 −18.988 1.00 23.04 A ATOM 2106 O ALA A 338 90.518 15.541 −19.800 1.00 22.63 A ATOM 2107 N HIS A 339 89.447 16.570 −18.131 1.00 23.26 A ATOM 2108 CA HIS A 339 90.362 17.705 −18.148 1.00 23.33 A ATOM 2109 CB HIS A 339 90.017 18.680 −17.027 1.00 22.99 A ATOM 2110 CG HIS A 339 90.696 20.004 −17.156 1.00 23.43 A ATOM 2111 CD2 HIS A 339 90.279 21.168 −17.710 1.00 24.32 A ATOM 2112 ND1 HIS A 339 91.993 20.219 −16.741 1.00 22.64 A ATOM 2113 CE1 HIS A 339 92.346 21.459 −17.036 1.00 24.03 A ATOM 2114 NE2 HIS A 339 91.324 22.056 −17.626 1.00 23.65 A ATOM 2115 C HIS A 339 91.833 17.302 −18.046 1.00 24.36 A ATOM 2116 O HIS A 339 92.186 16.376 −17.317 1.00 24.27 A ATOM 2117 N PRO A 340 92.713 17.999 −18.788 1.00 25.89 A ATOM 2118 CD PRO A 340 92.394 19.050 −19.777 1.00 26.27 A ATOM 2119 CA PRO A 340 94.151 17.714 −18.785 1.00 26.69 A ATOM 2120 CB PRO A 340 94.727 18.861 −19.613 1.00 26.46 A ATOM 2121 CG PRO A 340 93.654 19.090 −20.636 1.00 25.56 A ATOM 2122 C PRO A 340 94.772 17.629 −17.396 1.00 27.13 A ATOM 2123 O PRO A 340 95.686 16.841 −17.167 1.00 28.89 A ATOM 2124 N PHE A 341 94.281 18.438 −16.466 1.00 26.76 A ATOM 2125 CA PHE A 341 94.815 18.417 −15.110 1.00 25.83 A ATOM 2126 CB PHE A 341 94.100 19.451 −14.239 1.00 24.58 A ATOM 2127 CG PHE A 341 94.628 19.527 −12.835 1.00 23.75 A ATOM 2128 CD1 PHE A 341 95.890 20.060 −12.578 1.00 24.62 A ATOM 2129 CD2 PHE A 341 93.867 19.066 −11.765 1.00 24.82 A ATOM 2130 CE1 PHE A 341 96.386 20.136 −11.273 1.00 23.48 A ATOM 2131 CE2 PHE A 341 94.352 19.136 −10.454 1.00 23.61 A ATOM 2132 CZ PHE A 341 95.614 19.673 −10.209 1.00 23.80 A ATOM 2133 C PHE A 341 94.684 17.039 −14.458 1.00 25.53 A ATOM 2134 O PHE A 341 95.453 16.698 −13.572 1.00 25.60 A ATOM 2135 N PHE A 342 93.718 16.248 −14.905 1.00 26.56 A ATOM 2136 CA PHE A 342 93.486 14.928 −14.327 1.00 28.32 A ATOM 2137 CB PHE A 342 91.992 14.724 −14.095 1.00 25.63 A ATOM 2138 CG PHE A 342 91.374 15.731 −13.169 1.00 24.19 A ATOM 2139 CD1 PHE A 342 91.830 15.868 −11.859 1.00 24.72 A ATOM 2140 CD2 PHE A 342 90.285 16.492 −13.579 1.00 21.46 A ATOM 2141 CE1 PHE A 342 91.200 16.744 −10.969 1.00 22.95 A ATOM 2142 CE2 PHE A 342 89.649 17.368 −12.699 1.00 19.82 A ATOM 2143 CZ PHE A 342 90.105 17.491 −11.393 1.00 20.87 A ATOM 2144 C PHE A 342 94.009 13.811 −15.217 1.00 31.08 A ATOM 2145 O PHE A 342 93.655 12.643 −15.047 1.00 32.72 A ATOM 2146 N GLU A 343 94.863 14.183 −16.159 1.00 33.50 A ATOM 2147 CA GLU A 343 95.446 13.250 −17.114 1.00 36.10 A ATOM 2148 CB GLU A 343 96.738 13.853 −17.676 1.00 38.76 A ATOM 2149 CG GLU A 343 96.842 13.883 −19.194 1.00 44.39 A ATOM 2150 CD GLU A 343 96.911 15.307 −19.750 1.00 48.43 A ATOM 2151 OE1 GLU A 343 97.665 16.143 −19.190 1.00 47.87 A ATOM 2152 OE2 GLU A 343 96.217 15.587 −20.755 1.00 49.34 A ATOM 2153 C GLU A 343 95.747 11.855 −16.552 1.00 35.54 A ATOM 2154 O GLU A 343 95.210 10.847 −17.019 1.00 33.70 A ATOM 2155 N SER A 344 96.604 11.810 −15.539 1.00 34.66 A ATOM 2156 CA SER A 344 97.024 10.545 −14.950 1.00 33.91 A ATOM 2157 CB SER A 344 98.421 10.712 −14.360 1.00 33.13 A ATOM 2158 OG SER A 344 98.387 11.578 −13.242 1.00 30.32 A ATOM 2159 C SER A 344 96.116 9.927 −13.886 1.00 33.50 A ATOM 2160 O SER A 344 96.510 8.962 −13.234 1.00 32.98 A ATOM 2161 N VAL A 345 94.908 10.448 −13.713 1.00 31.80 A ATOM 2162 CA VAL A 345 94.021 9.903 −12.689 1.00 31.70 A ATOM 2163 CB VAL A 345 93.039 10.981 −12.152 1.00 31.20 A ATOM 2164 CG1 VAL A 345 92.153 10.375 −11.079 1.00 29.96 A ATOM 2165 CG2 VAL A 345 93.799 12.176 −11.601 1.00 27.23 A ATOM 2166 C VAL A 345 93.175 8.707 −13.133 1.00 32.88 A ATOM 2167 O VAL A 345 92.597 8.712 −14.223 1.00 32.39 A ATOM 2168 N THR A 346 93.109 7.688 −12.279 1.00 31.88 A ATOM 2169 CA THR A 346 92.285 6.511 −12.539 1.00 32.94 A ATOM 2170 CB THR A 346 93.007 5.209 −12.149 1.00 35.61 A ATOM 2171 OG1 THR A 346 94.137 5.012 −13.013 1.00 37.85 A ATOM 2172 CG2 THR A 346 92.060 4.022 −12.267 1.00 32.32 A ATOM 2173 C THR A 346 91.051 6.700 −11.658 1.00 33.08 A ATOM 2174 O THR A 346 91.083 6.460 −10.448 1.00 34.21 A ATOM 2175 N TRP A 347 89.964 7.142 −12.274 1.00 31.78 A ATOM 2176 CA TRP A 347 88.741 7.427 −11.549 1.00 31.53 A ATOM 2177 CB TRP A 347 87.769 8.171 −12.463 1.00 28.28 A ATOM 2178 CG TRP A 347 88.303 9.476 −12.937 1.00 23.66 A ATOM 2179 CD2 TRP A 347 88.263 10.722 −12.231 1.00 23.03 A ATOM 2180 CE2 TRP A 347 88.927 11.678 −13.031 1.00 20.77 A ATOM 2181 CE3 TRP A 347 87.731 11.121 −10.999 1.00 20.57 A ATOM 2182 CD1 TRP A 347 88.969 9.718 −14.102 1.00 21.92 A ATOM 2183 NE1 TRP A 347 89.348 11.041 −14.168 1.00 22.23 A ATOM 2184 CZ2 TRP A 347 89.074 13.008 −12.640 1.00 21.04 A ATOM 2185 CZ3 TRP A 347 87.876 12.444 −10.611 1.00 20.11 A ATOM 2186 CH2 TRP A 347 88.544 13.372 −11.430 1.00 20.44 A ATOM 2187 C TRP A 347 88.014 6.267 −10.899 1.00 34.19 A ATOM 2188 O TRP A 347 87.382 6.440 −9.854 1.00 34.97 A ATOM 2189 N GLU A 348 88.108 5.089 −11.502 1.00 35.77 A ATOM 2190 CA GLU A 348 87.405 3.913 −11.000 1.00 36.41 A ATOM 2191 CB GLU A 348 87.600 2.740 −11.977 1.00 36.95 A ATOM 2192 CG GLU A 348 88.990 2.626 −12.588 0.00 36.86 A ATOM 2193 CD GLU A 348 89.173 3.510 −13.812 0.00 36.91 A ATOM 2194 OE1 GLU A 348 89.119 4.750 −13.677 0.00 36.92 A ATOM 2195 OE2 GLU A 348 89.370 2.960 −14.916 0.00 36.92 A ATOM 2196 C GLU A 348 87.668 3.435 −9.563 1.00 36.38 A ATOM 2197 O GLU A 348 86.773 2.866 −8.935 1.00 38.29 A ATOM 2198 N ASN A 349 88.857 3.669 −9.019 1.00 34.41 A ATOM 2199 CA ASN A 349 89.134 3.182 −7.668 1.00 33.02 A ATOM 2200 CB ASN A 349 89.848 1.844 −7.765 1.00 34.07 A ATOM 2201 CG ASN A 349 91.220 1.978 −8.381 1.00 35.48 A ATOM 2202 OD1 ASN A 349 91.409 2.742 −9.324 1.00 35.13 A ATOM 2203 ND2 ASN A 349 92.188 1.235 −7.852 1.00 38.04 A ATOM 2204 C ASN A 349 89.970 4.116 −6.804 1.00 30.73 A ATOM 2205 O ASN A 349 90.878 3.672 −6.106 1.00 30.66 A ATOM 2206 N LEU A 350 89.662 5.403 −6.850 1.00 28.42 A ATOM 2207 CA LEU A 350 90.390 6.397 −6.072 1.00 27.13 A ATOM 2208 CB LEU A 350 89.655 7.737 −6.128 1.00 25.19 A ATOM 2209 CG LEU A 350 89.803 8.543 −7.418 1.00 25.97 A ATOM 2210 CD1 LEU A 350 88.841 9.732 −7.428 1.00 26.30 A ATOM 2211 CD2 LEU A 350 91.242 9.014 −7.521 1.00 27.40 A ATOM 2212 C LEU A 350 90.581 5.999 −4.614 1.00 26.30 A ATOM 2213 O LEU A 350 91.645 6.201 −4.036 1.00 26.73 A ATOM 2214 N HIS A 351 89.547 5.424 −4.024 1.00 27.16 A ATOM 2215 CA HIS A 351 89.593 5.044 −2.622 1.00 28.60 A ATOM 2216 CB HIS A 351 88.184 4.748 −2.124 1.00 29.94 A ATOM 2217 CG HIS A 351 88.111 4.503 −0.653 1.00 30.99 A ATOM 2218 CD2 HIS A 351 88.324 5.329 0.399 1.00 31.86 A ATOM 2219 ND1 HIS A 351 87.790 3.275 −0.118 1.00 29.43 A ATOM 2220 CE1 HIS A 351 87.804 3.356 1.202 1.00 31.81 A ATOM 2221 NE2 HIS A 351 88.125 4.592 1.541 1.00 32.90 A ATOM 2222 C HIS A 351 90.509 3.873 −2.298 1.00 28.99 A ATOM 2223 O HIS A 351 90.875 3.677 −1.141 1.00 28.53 A ATOM 2224 N GLN A 352 90.865 3.088 −3.307 1.00 30.57 A ATOM 2225 CA GLN A 352 91.764 1.959 −3.095 1.00 33.42 A ATOM 2226 CB GLN A 352 91.563 0.880 −4.162 1.00 35.01 A ATOM 2227 CG GLN A 352 90.696 −0.289 −3.737 1.00 37.07 A ATOM 2228 CD GLN A 352 89.275 0.123 −3.474 1.00 39.83 A ATOM 2229 OE1 GLN A 352 88.676 0.856 −4.267 1.00 41.90 A ATOM 2230 NE2 GLN A 352 88.712 −0.351 −2.365 1.00 39.86 A ATOM 2231 C GLN A 352 93.197 2.457 −3.173 1.00 33.85 A ATOM 2232 O GLN A 352 94.126 1.782 −2.734 1.00 35.32 A ATOM 2233 N GLN A 353 93.368 3.647 −3.734 1.00 32.53 A ATOM 2234 CA GLN A 353 94.693 4.216 −3.886 1.00 32.78 A ATOM 2235 CB GLN A 353 94.666 5.298 −4.965 1.00 32.07 A ATOM 2236 CG GLN A 353 94.373 4.739 −6.345 1.00 31.94 A ATOM 2237 CD GLN A 353 94.206 5.819 −7.382 1.00 32.50 A ATOM 2238 OE1 GLN A 353 95.008 6.749 −7.452 1.00 35.33 A ATOM 2239 NE2 GLN A 353 93.167 5.701 −8.204 1.00 31.02 A ATOM 2240 C GLN A 353 95.246 4.779 −2.588 1.00 33.27 A ATOM 2241 O GLN A 353 94.494 5.209 −1.717 1.00 32.38 A ATOM 2242 N THR A 354 96.570 4.746 −2.462 1.00 33.29 A ATOM 2243 CA THR A 354 97.239 5.267 −1.280 1.00 34.35 A ATOM 2244 CB THR A 354 98.615 4.601 −1.069 1.00 35.88 A ATOM 2245 OG1 THR A 354 98.430 3.232 −0.690 1.00 36.70 A ATOM 2246 CG2 THR A 354 99.403 5.325 0.027 1.00 36.08 A ATOM 2247 C THR A 354 97.440 6.760 −1.478 1.00 33.06 A ATOM 2248 O THR A 354 98.120 7.181 −2.403 1.00 31.33 A ATOM 2249 N PRO A 355 96.844 7.581 −0.604 1.00 33.40 A ATOM 2250 CD PRO A 355 96.000 7.220 0.544 1.00 31.90 A ATOM 2251 CA PRO A 355 96.974 9.035 −0.710 1.00 34.90 A ATOM 2252 CB PRO A 355 96.156 9.543 0.475 1.00 33.68 A ATOM 2253 CG PRO A 355 95.160 8.452 0.698 1.00 33.37 A ATOM 2254 C PRO A 355 98.428 9.475 −0.623 1.00 36.27 A ATOM 2255 O PRO A 355 99.196 8.960 0.191 1.00 35.70 A ATOM 2256 N PRO A 356 98.824 10.433 −1.464 1.00 37.66 A ATOM 2257 CD PRO A 356 98.010 11.198 −2.423 1.00 38.22 A ATOM 2258 CA PRO A 356 100.205 10.916 −1.441 1.00 39.93 A ATOM 2259 CB PRO A 356 100.227 11.944 −2.570 1.00 38.83 A ATOM 2260 CG PRO A 356 98.818 12.466 −2.580 1.00 38.26 A ATOM 2261 C PRO A 356 100.532 11.534 −0.085 1.00 41.87 A ATOM 2262 O PRO A 356 99.696 12.209 0.506 1.00 40.91 A ATOM 2263 N ALA A 357 101.741 11.286 0.409 1.00 46.23 A ATOM 2264 CA ALA A 357 102.160 11.837 1.691 1.00 51.16 A ATOM 2265 CB ALA A 357 103.587 11.410 2.001 1.00 49.78 A ATOM 2266 C ALA A 357 102.077 13.354 1.589 1.00 54.64 A ATOM 2267 O ALA A 357 102.591 13.942 0.637 1.00 55.14 A ATOM 2268 N LEU A 358 101.419 13.985 2.559 1.00 58.59 A ATOM 2269 CA LEU A 358 101.276 15.437 2.552 1.00 62.92 A ATOM 2270 CB LEU A 358 100.107 15.866 3.441 1.00 62.51 A ATOM 2271 CG LEU A 358 98.732 15.752 2.783 1.00 63.05 A ATOM 2272 CD1 LEU A 358 97.657 16.251 3.737 1.00 63.34 A ATOM 2273 CD2 LEU A 358 98.721 16.570 1.494 1.00 62.56 A ATOM 2274 C LEU A 358 102.536 16.173 2.984 1.00 65.81 A ATOM 2275 O LEU A 358 102.675 16.559 4.148 1.00 66.45 A ATOM 2276 N THR A 359 103.441 16.368 2.025 1.00 69.31 A ATOM 2277 CA THR A 359 104.715 17.057 2.236 1.00 72.25 A ATOM 2278 CB THR A 359 104.519 18.594 2.271 1.00 73.17 A ATOM 2279 OG1 THR A 359 103.564 18.937 3.284 1.00 75.38 A ATOM 2280 CG2 THR A 359 104.030 19.101 0.916 1.00 72.93 A ATOM 2281 C THR A 359 105.468 16.627 3.497 1.00 73.76 A ATOM 2282 O THR A 359 105.011 15.683 4.180 1.00 74.61 A ATOM 2283 OXT THR A 359 106.523 17.237 3.780 1.00 75.50 A ATOM 2284 OH2 TIP S 1 82.965 32.402 −3.946 1.00 13.32 S ATOM 2285 OH2 TIP S 2 91.556 13.784 −17.557 1.00 22.11 S ATOM 2286 OH2 TIP S 3 87.391 33.155 −1.722 1.00 22.84 S ATOM 2287 OH2 TIP S 4 69.033 3.499 13.879 1.00 22.91 S ATOM 2288 OH2 TIP S 5 81.088 19.368 −18.406 1.00 24.13 S ATOM 2289 OH2 TIP S 6 75.641 16.130 8.209 1.00 26.44 S ATOM 2290 OH2 TIP S 7 74.760 20.961 3.347 1.00 27.74 S ATOM 2291 OH2 TIP S 8 75.152 6.784 5.545 1.00 22.53 S ATOM 2292 OH2 TIP S 9 77.282 11.807 −17.666 1.00 35.96 S ATOM 2293 OH2 TIP S 10 81.785 8.968 −8.072 1.00 25.44 S ATOM 2294 OH2 TIP S 11 78.609 24.424 −2.074 1.00 22.05 S ATOM 2295 OH2 TIP S 12 94.883 8.256 −9.981 1.00 37.17 S ATOM 2296 OH2 TIP S 13 73.164 38.970 −1.072 1.00 35.95 S ATOM 2297 OH2 TIP S 14 78.806 27.556 −3.116 1.00 39.27 S ATOM 2298 OH2 TIP S 15 89.050 8.041 10.604 1.00 23.40 S ATOM 2299 OH2 TIP S 16 73.265 40.376 −3.301 1.00 26.94 S ATOM 2300 OH2 TIP S 18 84.081 33.371 4.243 1.00 30.61 S ATOM 2301 OH2 TIP S 19 78.571 −0.530 16.531 1.00 26.61 S ATOM 2302 OH2 TIP S 21 70.088 3.703 17.559 1.00 28.94 S ATOM 2303 OH2 TIP S 22 79.212 13.330 −18.791 1.00 26.94 S ATOM 2304 OH2 TIP S 23 91.672 10.665 −16.153 1.00 30.26 S ATOM 2305 OH2 TIP S 25 104.173 17.689 −7.204 1.00 31.65 S ATOM 2306 OH2 TIP S 27 87.578 18.354 −20.604 1.00 25.98 S ATOM 2307 OH2 TIP S 28 82.272 34.870 −16.021 1.00 27.40 S ATOM 2308 OH2 TIP S 29 100.496 13.074 −9.812 1.00 37.92 S ATOM 2309 OH2 TIP S 30 65.147 10.515 28.440 1.00 40.03 S ATOM 2310 OH2 TIP S 31 90.721 38.800 −4.631 1.00 42.09 S ATOM 2311 OH2 TIP S 32 83.367 23.841 15.654 1.00 36.15 S ATOM 2312 OH2 TIP S 33 87.754 11.897 23.760 1.00 26.76 S ATOM 2313 OH2 TIP S 34 77.755 13.485 −15.395 1.00 31.85 S ATOM 2314 OH2 TIP S 35 79.767 43.115 5.371 1.00 35.26 S ATOM 2315 OH2 TIP S 37 80.173 32.998 6.198 1.00 40.03 S ATOM 2316 OH2 TIP S 40 85.958 19.110 24.502 1.00 24.42 S ATOM 2317 OH2 TIP S 42 77.719 −0.391 23.732 1.00 39.71 S ATOM 2318 OH2 TIP S 44 92.563 36.428 −5.574 1.00 35.43 S ATOM 2319 OH2 TIP S 45 90.942 34.092 3.570 1.00 43.64 S ATOM 2320 OH2 TIP S 46 74.357 32.157 −13.849 1.00 33.31 S ATOM 2321 OH2 TIP S 47 90.220 14.449 16.172 1.00 34.34 S ATOM 2322 OH2 TIP S 48 77.876 11.229 −13.863 1.00 23.53 S ATOM 2323 OH2 TIP S 50 76.289 12.589 −11.572 1.00 37.74 S ATOM 2324 OH2 TIP S 51 76.619 2.787 −2.969 1.00 35.95 S ATOM 2325 OH2 TIP S 52 65.118 19.629 24.370 1.00 34.85 S ATOM 2326 OH2 TIP S 53 99.690 31.473 −13.046 1.00 48.21 S ATOM 2327 OH2 TIP S 54 88.376 36.865 3.454 1.00 38.54 S ATOM 2328 OH2 TIP S 57 91.236 10.819 18.279 1.00 40.76 S ATOM 2329 OH2 TIP S 59 100.017 21.990 −14.622 1.00 41.65 S ATOM 2330 OH2 TIP S 63 87.188 25.521 11.438 1.00 41.53 S ATOM 2331 OH2 TIP S 65 90.264 19.625 12.286 1.00 24.22 S ATOM 2332 OH2 TIP S 66 83.805 26.254 −18.365 1.00 37.50 S ATOM 2333 OH2 TIP S 68 78.394 7.378 2.855 1.00 23.47 S ATOM 2334 OH2 TIP S 74 85.541 11.500 −18.436 1.00 37.35 S ATOM 2335 OH2 TIP S 76 98.981 8.707 2.808 1.00 47.34 S ATOM 2336 OH2 TIP S 78 87.802 19.118 22.522 1.00 39.99 S ATOM 2337 OH2 TIP S 80 92.438 3.105 2.517 1.00 37.27 S ATOM 2338 OH2 TIP S 81 75.580 −0.821 22.186 1.00 36.41 S ATOM 2339 OH2 TIP S 82 60.506 24.278 21.938 1.00 31.55 S ATOM 2340 OH2 TIP S 83 92.298 22.520 −21.183 1.00 42.32 S ATOM 2341 OH2 TIP S 84 74.351 4.211 −3.464 1.00 32.53 S ATOM 2342 OH2 TIP S 85 76.502 25.963 −21.839 1.00 41.89 S ATOM 2343 OH2 TIP S 86 97.965 13.142 9.216 1.00 41.76 S ATOM 2344 OH2 TIP S 87 78.657 4.418 3.361 1.00 35.63 S ATOM 2345 OH2 TIP S 88 93.633 28.572 3.429 1.00 34.30 S ATOM 2346 OH2 TIP S 89 104.691 20.306 −7.235 1.00 32.75 S ATOM 2347 OH2 TIP S 91 98.360 16.754 −15.558 1.00 37.92 S ATOM 2348 OH2 TIP S 92 88.175 32.723 −14.088 1.00 38.91 S ATOM 2349 OH2 TIP S 93 96.974 27.936 −17.613 1.00 34.47 S ATOM 2350 OH2 TIP S 94 85.585 22.346 15.199 1.00 41.12 S ATOM 2351 OH2 TIP S 100 80.948 −0.010 7.892 1.00 12.04 S ATOM 2352 OH2 TIP S 101 76.653 29.202 −3.527 1.00 22.10 S ATOM 2353 OH2 TIP S 102 74.980 8.979 −7.975 1.00 21.17 S ATOM 2354 OH2 TIP S 103 88.843 28.393 3.994 1.00 30.94 S ATOM 2355 OH2 TIP S 105 76.862 8.067 28.490 1.00 20.20 S ATOM 2356 OH2 TIP S 106 66.435 30.702 8.817 1.00 35.87 S ATOM 2357 OH2 TIP S 109 67.384 7.757 8.860 1.00 39.38 S ATOM 2358 OH2 TIP S 110 66.852 4.666 22.301 1.00 32.75 S ATOM 2359 OH2 TIP S 111 72.391 2.229 −3.501 1.00 51.07 S ATOM 2360 OH2 TIP S 116 80.209 7.061 −7.886 1.00 35.49 S ATOM 2361 OH2 TIP S 121 74.466 15.313 −12.357 1.00 45.36 S ATOM 2362 OH2 TIP S 122 79.225 28.627 0.179 1.00 30.68 S ATOM 2363 OH2 TIP S 124 59.090 22.126 22.498 1.00 35.94 S ATOM 2364 OH2 TIP S 126 73.715 24.448 −13.973 1.00 44.35 S ATOM 2365 OH2 TIP S 127 105.619 22.931 −11.256 1.00 43.80 S ATOM 2366 OH2 TIP S 128 86.658 32.319 −16.090 1.00 39.40 S ATOM 2367 OH2 TIP S 129 70.750 21.709 −10.875 1.00 45.74 S ATOM 2368 OH2 TIP S 136 77.820 12.663 6.090 1.00 47.18 S ATOM 2369 OH2 TIP S 142 90.942 35.947 −13.582 1.00 48.16 S ATOM 2370 OH2 TIP S 146 67.351 6.830 24.075 1.00 36.66 S ATOM 2371 OH2 TIP S 148 98.067 12.182 −7.216 1.00 38.66 S ATOM 2372 OH2 TIP S 156 75.211 13.809 −20.582 1.00 45.56 S ATOM 2373 OH2 TIP S 158 72.261 20.575 12.175 1.00 51.45 S ATOM 2374 OH2 TIP S 166 77.289 42.685 7.086 1.00 42.23 S ATOM 2375 OH2 TIP S 174 65.330 6.552 20.003 1.00 42.22 S ATOM 2376 OH2 TIP S 176 88.027 20.872 −20.665 1.00 35.09 S ATOM 2377 OH2 TIP S 178 99.488 29.517 −16.497 1.00 44.21 S ATOM 2378 OH2 TIP S 182 93.851 13.830 −20.448 1.00 50.19 S ATOM 2379 OH2 TIP S 192 83.811 26.388 9.460 1.00 39.52 S ATOM 2380 OH2 TIP S 193 91.704 42.080 2.405 1.00 40.67 S ATOM 2381 O12 GLC G 1 82.624 0.887 12.473 1.00 47.94 G ATOM 2382 C11 GLC G 1 82.240 2.160 13.000 1.00 48.49 G ATOM 2383 C13 GLC G 1 83.237 3.235 12.553 1.00 46.87 G ATOM 2384 O14 GLC G 1 84.544 2.903 13.022 1.00 46.62 G ATOM 2385 C15 GLC G 1 82.817 4.591 13.117 1.00 45.80 G ATOM 2386 O16 GLC G 1 83.746 5.589 12.703 1.00 43.50 G ATOM 2387 O12 GLC G 5 86.722 −2.593 0.107 1.00 39.62 G ATOM 2388 C11 GLC G 5 86.245 −1.364 −0.429 1.00 44.37 G ATOM 2389 C13 GLC G 5 86.764 −0.193 0.394 1.00 44.36 G ATOM 2390 O14 GLC G 5 86.355 −0.326 1.761 1.00 47.64 G ATOM 2391 C15 GLC G 5 86.231 1.132 −0.195 1.00 45.11 G ATOM 2392 O16 GLC G 5 86.666 1.310 −1.557 1.00 42.61 G ATOM 2393 O12 GLC G 8 87.512 4.414 −5.278 1.00 38.37 G ATOM 2394 C11 GLC G 8 86.362 5.220 −5.023 1.00 34.16 G ATOM 2395 C13 GLC G 8 85.750 5.654 −6.351 1.00 35.54 G ATOM 2396 O14 GLC G 8 86.717 6.392 −7.111 1.00 37.03 G ATOM 2397 C15 GLC G 8 84.521 6.523 −6.082 1.00 35.46 G ATOM 2398 O16 GLC G 8 83.948 6.931 −7.319 1.00 33.79 G ATOM 2399 C34 STO L 1 82.178 19.404 9.614 1.00 23.98 L ATOM 2400 O33 STO L 1 83.091 19.645 10.691 1.00 24.40 L ATOM 2401 C25 STO L 1 82.557 20.621 11.610 1.00 19.84 L ATOM 2402 C26 STO L 1 83.748 21.455 12.055 1.00 20.35 L ATOM 2403 N31 STO L 1 84.251 22.242 10.916 1.00 22.56 L ATOM 2404 C32 STO L 1 83.716 23.544 10.481 1.00 20.91 L ATOM 2405 C27 STO L 1 84.847 20.523 12.559 1.00 19.37 L ATOM 2406 C28 STO L 1 84.278 19.595 13.658 1.00 18.70 L ATOM 2407 O29 STO L 1 82.889 19.845 13.980 1.00 20.08 L ATOM 2408 C24 STO L 1 81.939 19.930 12.872 1.00 21.85 L ATOM 2409 C35 STO L 1 80.791 20.824 13.403 1.00 20.12 L ATOM 2410 N6 STO L 1 81.456 18.689 12.528 1.00 19.30 L ATOM 2411 C5 STO L 1 80.172 18.450 12.023 1.00 16.04 L ATOM 2412 C4 STO L 1 79.039 19.219 11.690 1.00 14.17 L ATOM 2413 C3 STO L 1 77.901 18.569 11.148 1.00 14.32 L ATOM 2414 C2 STO L 1 77.899 17.158 10.946 1.00 14.05 L ATOM 2415 C1 STO L 1 79.035 16.386 11.282 1.00 13.54 L ATOM 2416 C23 STO L 1 80.154 17.053 11.812 1.00 16.42 L ATOM 2417 C22 STO L 1 81.361 16.522 12.164 1.00 17.74 L ATOM 2418 C7 STO L 1 82.162 17.525 12.606 1.00 18.84 L ATOM 2419 C8 STO L 1 83.501 17.279 12.972 1.00 18.69 L ATOM 2420 N9 STO L 1 84.462 18.150 13.376 1.00 19.59 L ATOM 2421 C10 STO L 1 85.663 17.477 13.561 1.00 19.11 L ATOM 2422 C11 STO L 1 86.968 17.838 13.942 1.00 16.81 L ATOM 2423 C12 STO L 1 87.961 16.831 14.007 1.00 20.66 L ATOM 2424 C13 STO L 1 87.645 15.476 13.689 1.00 20.30 L ATOM 2425 C14 STO L 1 86.329 15.117 13.306 1.00 19.66 L ATOM 2426 C15 STO L 1 85.364 16.127 13.248 1.00 18.74 L ATOM 2427 C16 STO L 1 84.049 16.022 12.899 1.00 19.21 L ATOM 2428 C17 STO L 1 83.217 14.936 12.440 1.00 18.26 L ATOM 2429 C21 STO L 1 81.934 15.217 12.098 1.00 17.21 L ATOM 2430 C20 STO L 1 81.325 14.098 11.689 1.00 17.68 L ATOM 2431 N19 STO L 1 82.281 13.080 11.786 1.00 13.64 L ATOM 2432 C18 STO L 1 83.457 13.603 12.261 1.00 16.89 L ATOM 2433 O30 STO L 1 84.493 12.981 12.504 1.00 15.41 L ATOM 2434 S SO4 I 1 64.914 7.877 16.247 1.00 82.11 I ATOM 2435 O1 SO4 I 1 63.624 8.415 15.778 1.00 82.68 I ATOM 2436 O2 SO4 I 1 65.841 8.992 16.520 1.00 82.73 I ATOM 2437 O3 SO4 I 1 65.479 7.010 15.198 1.00 83.33 I ATOM 2438 O4 SO4 I 1 64.709 7.088 17.477 1.00 82.04 I ATOM 2439 S SO4 I 2 68.379 −7.029 19.810 1.00 112.82 I ATOM 2440 O1 SO4 I 2 66.992 −6.526 19.786 1.00 112.60 I ATOM 2441 O2 SO4 I 2 68.850 −7.226 18.425 1.00 112.21 I ATOM 2442 O3 SO4 I 2 68.426 −8.312 20.538 1.00 112.24 I ATOM 2443 O4 SO4 I 2 69.249 −6.051 20.491 1.00 112.72 I ATOM 2444 S SO4 I 3 84.927 −1.874 12.302 1.00 79.99 I ATOM 2445 O1 SO4 I 3 84.408 −1.334 13.568 1.00 79.90 I ATOM 2446 O2 SO4 I 3 84.442 −1.050 11.178 1.00 80.43 I ATOM 2447 O3 SO4 I 3 84.453 −3.263 12.131 1.00 79.92 I ATOM 2448 O4 SO4 I 3 86.402 −1.845 12.326 1.00 80.52 I ATOM 2449 S SO4 I 4 80.577 9.632 30.033 1.00 98.23 I ATOM 2450 O1 SO4 I 4 79.725 9.060 28.972 1.00 96.88 I ATOM 2451 O2 SO4 I 4 82.000 9.461 29.683 1.00 97.80 I ATOM 2452 O3 SO4 I 4 80.304 8.944 31.309 1.00 98.08 I ATOM 2453 O4 SO4 I 4 80.281 11.069 30.178 1.00 98.08 I ATOM 2454 S SO4 I 5 89.310 6.131 25.915 1.00 110.86 I ATOM 2455 O1 SO4 I 5 89.025 6.456 27.331 1.00 110.48 I ATOM 2456 O2 SO4 I 5 88.042 6.095 25.151 1.00 110.12 I ATOM 2457 O3 SO4 I 5 89.970 4.810 25.844 1.00 110.72 I ATOM 2458 O4 SO4 I 5 90.205 7.155 25.330 1.00 110.02 I ATOM 2459 O2 PO4 P 100 64.527 26.252 2.299 1.00 88.98 P ATOM 2460 O3 PO4 P 100 66.482 25.155 1.367 1.00 88.39 P ATOM 2461 O4 PO4 P 100 66.688 26.504 3.376 1.00 87.87 P ATOM 2462 O1 PO4 P 100 66.264 27.565 1.240 1.00 88.80 P ATOM 2463 P PO4 P 100 65.992 26.368 2.070 1.00 88.61 P ATOM 2464 CB LEU 145 73.932 8.398 8.961 0.50 21.29 AC2 ATOM 2465 CG LEU 145 72.901 8.606 10.076 0.50 21.65 AC2 ATOM 2466 CD1 LEU 145 71.904 9.671 9.655 0.50 21.60 AC2 ATOM 2467 CD2 LEU 145 72.195 7.298 10.388 0.50 19.61 AC2 ATOM 2468 CB ASN 214 88.968 8.625 7.173 0.50 22.34 AC2 ATOM 2469 CG ASN 214 89.705 8.084 5.975 0.50 22.01 AC2 ATOM 2470 OD1 ASN 214 89.240 7.153 5.320 0.50 22.82 AC2 ATOM 2471 ND2 ASN 214 90.859 8.660 5.678 0.50 22.69 AC2 ATOM 2472 CB ASP 216 93.187 5.546 5.379 0.50 25.98 AC2 ATOM 2473 CG ASP 216 91.789 5.828 4.895 0.50 27.09 AC2 ATOM 2474 OD1 ASP 216 91.587 6.896 4.290 0.50 28.49 AC2 ATOM 2475 OD2 ASP 216 90.896 4.982 5.110 0.50 28.20 AC2 END

Example 8 Co-Ordinates for PDK1 Fragment Co-Crystallised with UCN-01

REMARK coordinates from restrained individual B-factor refinement REMARK refinement resolution: 25.0-2.50 A REMARK starting r= 0.1919 free_r= 0.2582 REMARK final   r= 0.1894 free_r= 0.2567 REMARK B rmsd for bonded mainchain atoms= 1.412 target=1.5 REMARK B rmsd for bonded sidechain atoms=  2.205 target=2.0 REMARK B rmsd for angle mainchain atoms= 2.401 target=2.0 REMARK B rmsd for angle sidechain atoms=  3.256 target=2.5 REMARK rweight= 0.1000 (with wa= 3.1611) REMARK target= mlf steps= 30 REMARK sg= P3(2)21 a= 123.387 b= 123.387 c= 47.115 alpha= 90 beta= 90 gamma= 120 REMARK parameter file 1 : /ddl/david/refinement/MY_CNS/prot.par REMARK parameter file 2 : /ddl/david/refinement/MY_CNS/ucn01.par REMARK parameter file 3 : CNS_TOPPAR:water_rep.param REMARK parameter file 4 : CNS_TOPPAR:ion.param REMARK parameter file 5 : /dd1/david/refinement/MY_CNS/glycerol.par REMARK molecular structure file: . . /generate/generate.mtf REMARK input coordinates: . . /minimize/minimize.pdb REMARK reflection file= . ./. . /. ./data/cns.hkl REMARK ncs= none REMARK B-correction resolution: 6.0-2.50 REMARK initial B-factor correction applied to fobs: REMARK B11= −4.722 B22= 4.722 B33= 9.444 REMARK B12= −3.572 B13= 0.000 B23= 0.000 REMARK B-factor correction applied to coordinate array B: −0.193 REMARK bulk solvent: density level= 0.3837 e/A 3, B-factor= 40.9071 A 2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with |Fobs| > 10000 * rms(Fobs) rejected REMARK theoretical total number of refl. in resol. range: 14485 (100.0%) REMARK number of unobserved reflections (no entry or |F|=0): 101 (0.7%) REMARK number of reflections rejected: 0 (0.0%) REMARK total number of reflections used: 14384 (99.3%) REMARK number of reflections in working set: 13795 (95.2%) REMARK number of reflections in test set: 589 (4.1%) CRYST1 123.387 123.387 47.115 90.00 90.00 120.00 P 32 2 1 REMARK FILENAME=“bindindividual.pdb” REMARK DATE:25-Mar-2003 17:21:21 created by user: david REMARK VERSION:1.0 ATOM 1 CB ALA A 73 67.051 −3.293 12.591 1.00 59.77 A ATOM 2 C ALA A 73 67.941 −4.753 14.416 1.00 61.14 A ATOM 3 O ALA A 73 67.184 −5.270 15.240 1.00 61.61 A ATOM 4 N ALA A 73 66.523 −5.729 12.643 1.00 58.89 A ATOM 5 CA ALA A 73 67.564 −4.697 12.943 1.00 60.69 A ATOM 6 N PRO A 74 69.130 −4.241 14.770 1.00 61.63 A ATOM 7 CD PRO A 74 70.264 −3.830 13.918 1.00 61.72 A ATOM 8 CA PRO A 74 69.514 −4.278 16.187 1.00 61.34 A ATOM 9 CB PRO A 74 70.918 −3.663 16.181 1.00 61.79 A ATOM 10 CG PRO A 74 71.458 −4.072 14.818 1.00 61.47 A ATOM 11 C PRO A 74 68.523 −3.481 17.047 1.00 60.16 A ATOM 12 O PRO A 74 67.625 −2.817 16.519 1.00 60.77 A ATOM 13 N ALA A 75 68.680 −3.562 18.368 1.00 58.13 A ATOM 14 CA ALA A 75 67.815 −2.828 19.292 1.00 54.74 A ATOM 15 CB ALA A 75 68.048 −3.309 20.731 1.00 54.90 A ATOM 16 C ALA A 75 68.175 −1.349 19.177 1.00 51.85 A ATOM 17 O ALA A 75 69.313 −1.005 18.851 1.00 52.46 A ATOM 18 N LYS A 76 67.215 −0.473 19.427 1.00 46.96 A ATOM 19 CA LYS A 76 67.507 0.947 19.354 1.00 43.72 A ATOM 20 CB LYS A 76 66.270 1.756 19.744 1.00 42.81 A ATOM 21 CG LYS A 76 66.177 3.116 19.087 1.00 41.81 A ATOM 22 CD LYS A 76 65.926 2.983 17.590 1.00 40.56 A ATOM 23 CE LYS A 76 65.691 4.343 16.943 1.00 42.58 A ATOM 24 NZ LYS A 76 65.362 4.231 15.495 1.00 42.73 A ATOM 25 C LYS A 76 68.639 1.218 20.351 1.00 41.25 A ATOM 26 O LYS A 76 68.599 0.741 21.488 1.00 41.68 A ATOM 27 N LYS A 77 69.655 1.960 19.936 1.00 37.68 A ATOM 28 CA LYS A 77 70.748 2.255 20.849 1.00 35.10 A ATOM 29 CB LYS A 77 72.016 2.619 20.074 1.00 34.13 A ATOM 30 CG LYS A 77 72.427 1.570 19.053 1.00 32.68 A ATOM 31 CD LYS A 77 73.927 1.537 18.858 1.00 33.90 A ATOM 32 CE LYS A 77 74.366 0.471 17.849 1.00 31.40 A ATOM 33 NZ LYS A 77 73.796 −0.863 18.164 1.00 34.76 A ATOM 34 C LYS A 77 70.313 3.408 21.743 1.00 34.79 A ATOM 35 O LYS A 77 69.319 4.077 21.458 1.00 34.20 A ATOM 36 N ARG A 78 71.023 3.626 22.845 1.00 34.88 A ATOM 37 CA ARG A 78 70.687 4.723 23.759 1.00 34.62 A ATOM 38 CB ARG A 78 69.694 4.247 24.839 1.00 38.43 A ATOM 39 CG ARG A 78 70.027 2.884 25.353 1.00 42.71 A ATOM 40 CD ARG A 78 69.355 2.424 26.625 1.00 48.52 A ATOM 41 NE ARG A 78 70.365 1.702 27.412 1.00 56.10 A ATOM 42 CZ ARG A 78 70.428 0.355 27.518 1.00 57.88 A ATOM 43 NH1 ARG A 78 69.519 −0.397 26.838 1.00 58.45 A ATOM 44 NH2 ARG A 78 71.335 −0.195 28.369 1.00 59.23 A ATOM 45 C ARG A 78 71.967 5.330 24.382 1.00 32.26 A ATOM 46 O ARG A 78 73.066 4.777 24.278 1.00 31.42 A ATOM 47 N PRO A 79 71.844 6.509 24.997 1.00 30.46 A ATOM 48 CD PRO A 79 70.616 7.284 25.232 1.00 28.96 A ATOM 49 CA PRO A 79 72.997 7.172 25.609 1.00 30.38 A ATOM 50 CB PRO A 79 72.350 8.303 26.405 1.00 28.86 A ATOM 51 CG PRO A 79 71.169 8.642 25.568 1.00 27.83 A ATOM 52 C PRO A 79 73.889 6.287 26.468 1.00 29.47 A ATOM 53 O PRO A 79 75.108 6.377 26.391 1.00 29.57 A ATOM 54 N GLU A 80 73.268 5.435 27.279 1.00 29.77 A ATOM 55 CA GLU A 80 73.975 4.533 28.179 1.00 29.55 A ATOM 56 CB GLU A 80 72.980 3.768 29.043 1.00 32.88 A ATOM 57 CG GLU A 80 71.996 4.643 29.798 1.00 40.36 A ATOM 58 CD GLU A 80 71.014 5.367 28.879 1.00 44.21 A ATOM 59 OE1 GLU A 80 70.422 4.700 28.000 1.00 46.94 A ATOM 60 OE2 GLU A 80 70.828 6.598 29.038 1.00 45.47 A ATOM 61 C GLU A 80 74.872 3.524 27.479 1.00 28.32 A ATOM 62 O GLU A 80 75.709 2.894 28.126 1.00 28.20 A ATOM 63 N ASP A 81 74.698 3.342 26.168 1.00 26.28 A ATOM 64 CA ASP A 81 75.528 2.384 25.441 1.00 23.59 A ATOM 65 CB ASP A 81 74.834 1.888 24.184 1.00 25.08 A ATOM 66 CG ASP A 81 73.510 1.225 24.477 1.00 28.14 A ATOM 67 OD1 ASP A 81 73.369 0.625 25.578 1.00 29.12 A ATOM 68 OD2 ASP A 81 72.617 1.294 23.601 1.00 28.33 A ATOM 69 C ASP A 81 76.856 2.967 25.046 1.00 23.24 A ATOM 70 O ASP A 81 77.716 2.257 24.519 1.00 24.29 A ATOM 71 N PHE A 82 77.036 4.259 25.309 1.00 21.34 A ATOM 72 CA PHE A 82 78.272 4.930 24.946 1.00 20.86 A ATOM 73 CB PHE A 82 77.992 6.029 23.929 1.00 18.34 A ATOM 74 CG PHE A 82 77.355 5.536 22.683 1.00 19.18 A ATOM 75 CD1 PHE A 82 78.138 5.099 21.610 1.00 19.28 A ATOM 76 CD2 PHE A 82 75.974 5.462 22.588 1.00 17.82 A ATOM 77 CE1 PHE A 82 77.551 4.597 20.461 1.00 17.94 A ATOM 78 CE2 PHE A 82 75.371 4.961 21.449 1.00 19.08 A ATOM 79 CZ PHE A 82 76.164 4.525 20.376 1.00 20.45 A ATOM 80 C PHE A 82 78.982 5.555 26.105 1.00 21.71 A ATOM 81 O PHE A 82 78.418 5.739 27.173 1.00 24.82 A ATOM 82 N LYS A 83 80.244 5.865 25.869 1.00 21.83 A ATOM 83 CA LYS A 83 81.077 6.555 26.823 1.00 22.27 A ATOM 84 CB LYS A 83 82.327 5.750 27.148 1.00 24.03 A ATOM 85 CG LYS A 83 83.074 6.320 28.340 1.00 30.99 A ATOM 86 CD LYS A 83 84.465 6.827 27.993 1.00 35.16 A ATOM 87 CE LYS A 83 85.465 5.683 27.945 1.00 39.06 A ATOM 88 NZ LYS A 83 85.512 4.974 29.266 1.00 41.00 A ATOM 89 C LYS A 83 81.462 7.775 25.998 1.00 22.51 A ATOM 90 O LYS A 83 82.324 7.677 25.120 1.00 23.24 A ATOM 91 N PHE A 84 80.800 8.907 26.227 1.00 20.27 A ATOM 92 CA PHE A 84 81.118 10.098 25.454 1.00 19.31 A ATOM 93 CB PHE A 84 80.016 11.145 25.605 1.00 19.95 A ATOM 94 CG PHE A 84 78.683 10.694 25.075 1.00 20.81 A ATOM 95 CD1 PHE A 84 77.855 9.879 25.835 1.00 21.62 A ATOM 96 CD2 PHE A 84 78.278 11.035 23.804 1.00 20.47 A ATOM 97 CE1 PHE A 84 76.665 9.418 25.339 1.00 19.26 A ATOM 98 CE2 PHE A 84 77.073 10.568 23.300 1.00 18.97 A ATOM 99 CZ PHE A 84 76.276 9.764 24.068 1.00 19.78 A ATOM 100 C PHE A 84 82.463 10.680 25.863 1.00 19.58 A ATOM 101 O PHE A 84 82.888 10.540 26.998 1.00 20.60 A ATOM 102 N GLY A 85 83.141 11.307 24.913 1.00 19.33 A ATOM 103 CA GLY A 85 84.434 11.909 25.169 1.00 18.23 A ATOM 104 C GLY A 85 84.480 13.368 24.743 1.00 19.96 A ATOM 105 O GLY A 85 83.533 14.124 24.962 1.00 20.02 A ATOM 106 N LYS A 86 85.568 13.764 24.101 1.00 20.79 A ATOM 107 CA LYS A 86 85.736 15.159 23.704 1.00 22.45 A ATOM 108 CB LYS A 86 87.168 15.400 23.210 1.00 22.06 A ATOM 109 CG LYS A 86 87.399 15.048 21.751 1.00 23.37 A ATOM 110 CD LYS A 86 88.832 14.591 21.505 1.00 26.45 A ATOM 111 CE LYS A 86 89.451 15.275 20.294 1.00 30.25 A ATOM 112 NZ LYS A 86 89.771 16.721 20.553 1.00 33.08 A ATOM 113 C LYS A 86 84.750 15.668 22.661 1.00 21.50 A ATOM 114 O LYS A 86 84.154 14.900 21.916 1.00 21.98 A ATOM 115 N ILE A 87 84.582 16.985 22.647 1.00 20.15 A ATOM 116 CA ILE A 87 83.712 17.661 21.705 1.00 19.38 A ATOM 117 CB ILE A 87 83.270 19.037 22.272 1.00 17.37 A ATOM 118 CG2 ILE A 87 82.724 19.935 21.163 1.00 15.07 A ATOM 119 CG1 ILE A 87 82.222 18.800 23.371 1.00 18.62 A ATOM 120 CD1 ILE A 87 81.848 20.025 24.190 1.00 16.91 A ATOM 121 C ILE A 87 84.549 17.836 20.436 1.00 19.85 A ATOM 122 O ILE A 87 85.666 18.317 20.502 1.00 21.66 A ATOM 123 N LEU A 88 84.030 17.406 19.293 1.00 19.65 A ATOM 124 CA LEU A 88 84.771 17.539 18.047 1.00 20.20 A ATOM 125 CB LEU A 88 84.423 16.405 17.078 1.00 18.76 A ATOM 126 CG LEU A 88 84.807 14.981 17.493 1.00 16.99 A ATOM 127 CD1 LEU A 88 84.122 13.995 16.570 1.00 13.92 A ATOM 128 CD2 LEU A 88 86.305 14.809 17.441 1.00 11.51 A ATOM 129 C LEU A 88 84.429 18.861 17.407 1.00 20.87 A ATOM 130 O LEU A 88 85.233 19.443 16.709 1.00 21.48 A ATOM 131 N GLY A 89 83.221 19.339 17.639 1.00 22.34 A ATOM 132 CA GLY A 89 82.856 20.601 17.043 1.00 25.87 A ATOM 133 C GLY A 89 81.476 21.057 17.451 1.00 29.45 A ATOM 134 O GLY A 89 80.673 20.292 17.990 1.00 29.48 A ATOM 135 N GLU A 90 81.196 22.321 17.188 1.00 32.71 A ATOM 136 CA GLU A 90 79.904 22.864 17.530 1.00 37.61 A ATOM 137 CB GLU A 90 80.047 23.798 18.738 1.00 38.05 A ATOM 138 CG GLU A 90 80.123 22.998 20.037 1.00 42.04 A ATOM 139 CD GLU A 90 80.463 23.813 21.270 1.00 45.47 A ATOM 140 OE1 GLU A 90 81.662 24.137 21.477 1.00 47.26 A ATOM 141 OE2 GLU A 90 79.524 24.119 22.041 1.00 47.39 A ATOM 142 C GLU A 90 79.277 23.565 16.349 1.00 40.01 A ATOM 143 O GLU A 90 79.972 24.148 15.518 1.00 42.05 A ATOM 144 N GLY A 91 77.962 23.440 16.240 1.00 42.05 A ATOM 145 CA GLY A 91 77.238 24.102 15.174 1.00 43.15 A ATOM 146 C GLY A 91 76.276 25.035 15.892 1.00 45.06 A ATOM 147 O GLY A 91 76.317 25.149 17.134 1.00 43.58 A ATOM 148 N SER A 92 75.408 25.699 15.136 1.00 46.66 A ATOM 149 CA SER A 92 74.430 26.606 15.742 1.00 48.21 A ATOM 150 CB SER A 92 73.754 27.462 14.660 1.00 51.13 A ATOM 151 CG SER A 92 73.601 26.741 13.439 1.00 54.79 A ATOM 152 C SER A 92 73.382 25.827 16.538 1.00 47.10 A ATOM 153 O SER A 92 73.055 26.190 17.678 1.00 49.44 A ATOM 154 N PHE A 93 72.874 24.743 15.957 1.00 44.39 A ATOM 155 CA PHE A 93 71.866 23.942 16.648 1.00 41.99 A ATOM 156 CB PHE A 93 70.617 23.798 15.780 1.00 43.92 A ATOM 157 CG PHE A 93 70.434 24.919 14.814 1.00 47.66 A ATOM 158 CD1 PHE A 93 70.689 24.729 13.455 1.00 49.35 A ATOM 159 CD2 PHE A 93 70.061 26.185 15.264 1.00 49.16 A ATOM 160 CE1 PHE A 93 70.581 25.789 12.551 1.00 51.11 A ATOM 161 CE2 PHE A 93 69.949 27.257 14.374 1.00 50.58 A ATOM 162 CZ PHE A 93 70.209 27.062 13.014 1.00 51.37 A ATOM 163 C PHE A 93 72.352 22.555 17.028 1.00 38.35 A ATOM 164 O PHE A 93 71.532 21.670 17.257 1.00 38.33 A ATOM 165 N SER A 94 73.665 22.351 17.106 1.00 33.28 A ATOM 166 CA SER A 94 74.151 21.028 17.440 1.00 29.57 A ATOM 167 CB SER A 94 73.996 20.106 16.227 1.00 30.45 A ATOM 168 OG SER A 94 75.123 20.190 15.368 1.00 30.51 A ATOM 169 C SER A 94 75.588 20.952 17.936 1.00 27.66 A ATOM 170 O SER A 94 76.369 21.893 17.803 1.00 27.25 A ATOM 171 N THR A 95 75.927 19.807 18.512 1.00 25.06 A ATOM 172 CA THR A 95 77.264 19.572 19.027 1.00 23.70 A ATOM 173 CB THR A 95 77.310 19.626 20.582 1.00 24.12 A ATOM 174 OG1 THR A 95 76.801 20.886 21.044 1.00 25.68 A ATOM 175 CG2 THR A 95 78.731 19.458 21.073 1.00 22.92 A ATOM 176 C THR A 95 77.655 18.180 18.594 1.00 22.05 A ATOM 177 O THR A 95 76.860 17.250 18.673 1.00 21.43 A ATOM 178 N VAL A 96 78.883 18.029 18.129 1.00 21.52 A ATOM 179 CA VAL A 96 79.348 16.723 17.702 1.00 19.53 A ATOM 180 CB VAL A 96 79.980 16.818 16.316 1.00 19.24 A ATOM 181 CG1 VAL A 96 80.418 15.443 15.839 1.00 17.73 A ATOM 182 CG2 VAL A 96 78.983 17.442 15.353 1.00 18.03 A ATOM 183 C VAL A 96 80.364 16.242 18.722 1.00 19.43 A ATOM 184 O VAL A 96 81.372 16.910 18.959 1.00 19.84 A ATOM 185 N VAL A 97 80.099 15.082 19.324 1.00 17.90 A ATOM 186 CA VAL A 97 80.989 14.532 20.341 1.00 17.32 A ATOM 187 CB VAL A 97 80.283 14.438 21.736 1.00 18.35 A ATOM 188 CG1 VAL A 97 79.581 15.750 22.066 1.00 20.10 A ATOM 189 CG2 VAL A 97 79.234 13.357 21.713 1.00 23.78 A ATOM 190 C VAL A 97 81.471 13.144 19.949 1.00 17.15 A ATOM 191 O VAL A 97 80.727 12.351 19.379 1.00 18.17 A ATOM 192 N LEU A 98 82.735 12.866 20.243 1.00 17.34 A ATOM 193 CA LEU A 98 83.331 11.575 19.974 1.00 17.44 A ATOM 194 CB LEU A 98 84.853 11.689 19.990 1.00 17.84 A ATOM 195 CG LEU A 98 85.656 10.407 19.737 1.00 18.59 A ATOM 196 CD1 LEU A 98 85.259 9.803 18.387 1.00 18.87 A ATOM 197 CD2 LEU A 98 87.151 10.738 19.772 1.00 16.62 A ATOM 198 C LEU A 98 82.874 10.626 21.081 1.00 18.35 A ATOM 199 O LEU A 98 82.992 10.926 22.259 1.00 18.60 A ATOM 200 N ALA A 99 82.340 9.476 20.697 1.00 19.15 A ATOM 201 CA ALA A 99 81.888 8.513 21.675 1.00 19.73 A ATOM 202 CB ALA A 99 80.383 8.534 21.759 1.00 17.97 A ATOM 203 C ALA A 99 82.360 7.117 21.317 1.00 21.86 A ATOM 204 O ALA A 99 82.502 6.766 20.131 1.00 22.18 A ATOM 205 N ARG A 100 82.631 6.324 22.345 1.00 21.93 A ATOM 206 CA ARG A 100 83.025 4.963 22.102 1.00 23.29 A ATOM 207 CB ARG A 100 84.333 4.637 22.805 1.00 25.99 A ATOM 208 CG ARG A 100 84.870 3.271 22.388 1.00 31.56 A ATOM 209 CD ARG A 100 86.146 2.923 23.129 1.00 35.19 A ATOM 210 NE ARG A 100 87.220 3.875 22.847 1.00 37.39 A ATOM 211 CZ ARG A 100 87.958 3.870 21.740 1.00 38.05 A ATOM 212 NH1 ARG A 100 87.742 2.953 20.797 1.00 37.25 A ATOM 213 NH2 ARG A 100 88.918 4.780 21.580 1.00 36.22 A ATOM 214 C ARG A 100 81.904 4.060 22.603 1.00 22.07 A ATOM 215 O ARG A 100 81.460 4.177 23.743 1.00 22.10 A ATOM 216 N GLU A 101 81.417 3.189 21.734 1.00 21.29 A ATOM 217 CA GLU A 101 80.357 2.262 22.119 1.00 22.87 A ATOM 218 CB GLU A 101 79.747 1.631 20.867 1.00 23.10 A ATOM 219 CG GLU A 101 78.740 0.563 21.148 1.00 22.71 A ATOM 220 CD GLU A 101 78.128 0.040 19.878 1.00 23.56 A ATOM 221 OE1 GLU A 101 78.892 −0.198 18.922 1.00 21.84 A ATOM 222 OE2 GLU A 101 76.890 −0.143 19.832 1.00 26.29 A ATOM 223 C GLU A 101 80.942 1.176 23.037 1.00 21.56 A ATOM 224 O GLU A 101 81.884 0.485 22.666 1.00 20.69 A ATOM 225 N LEU A 102 80.389 1.042 24.236 1.00 21.11 A ATOM 226 CA LEU A 102 80.874 0.057 25.204 1.00 21.54 A ATOM 227 CB LEU A 102 80.075 0.199 26.507 1.00 20.90 A ATOM 228 CG LEU A 102 80.193 1.620 27.092 1.00 22.35 A ATOM 229 CD1 LEU A 102 79.177 1.798 28.207 1.00 20.18 A ATOM 230 CD2 LEU A 102 81.600 1.866 27.608 1.00 17.47 A ATOM 231 C LEU A 102 80.896 −1.415 24.729 1.00 20.27 A ATOM 232 O LEU A 102 81.922 −2.078 24.825 1.00 21.63 A ATOM 233 N ALA A 103 79.792 −1.922 24.201 1.00 18.37 A ATOM 234 CA ALA A 103 79.757 −3.307 23.731 1.00 20.54 A ATOM 235 CB ALA A 103 78.333 −3.694 23.359 1.00 19.31 A ATOM 236 C ALA A 103 80.688 −3.658 22.552 1.00 22.26 A ATOM 237 O ALA A 103 81.002 −4.829 22.358 1.00 23.93 A ATOM 238 N THR A 104 81.141 −2.677 21.775 1.00 20.79 A ATOM 239 CA THR A 104 81.972 −2.999 20.622 1.00 21.40 A ATOM 240 CB THR A 104 81.279 −2.632 19.326 1.00 20.97 A ATOM 241 OG1 THR A 104 81.174 −1.205 19.259 1.00 23.21 A ATOM 242 CG2 THR A 104 79.891 −3.266 19.245 1.00 19.82 A ATOM 243 C THR A 104 83.304 −2.300 20.569 1.00 23.57 A ATOM 244 O THR A 104 84.168 −2.687 19.796 1.00 23.41 A ATOM 245 N SER A 105 83.454 −1.243 21.359 1.00 24.64 A ATOM 246 CA SER A 105 84.687 −0.487 21.390 1.00 24.23 A ATOM 247 CB SER A 105 85.855 −1.467 21.481 1.00 25.40 A ATOM 248 OG SER A 105 87.074 −0.788 21.719 1.00 34.15 A ATOM 249 C SER A 105 84.819 0.454 20.163 1.00 23.42 A ATOM 250 O SER A 105 85.803 1.187 20.013 1.00 23.28 A ATOM 251 N ARG A 106 83.821 0.448 19.295 1.00 21.19 A ATOM 252 CA ARG A 106 83.850 1.323 18.115 1.00 22.25 A ATOM 253 CB ARG A 106 82.754 0.922 17.118 1.00 24.82 A ATOM 254 CG ARG A 106 83.027 −0.343 16.349 1.00 25.20 A ATOM 255 CD ARG A 106 81.740 −0.942 15.884 1.00 25.19 A ATOM 256 NE ARG A 106 81.972 −1.900 14.815 1.00 26.11 A ATOM 257 CZ ARG A 106 81.042 −2.707 14.322 1.00 24.24 A ATOM 258 NH1 ARG A 106 79.805 −2.677 14.818 1.00 21.06 A ATOM 259 NH2 ARG A 106 81.351 −3.513 13.315 1.00 20.25 A ATOM 260 C ARG A 106 83.655 2.806 18.433 1.00 19.79 A ATOM 261 O ARG A 106 82.836 3.175 19.266 1.00 18.73 A ATOM 262 N GLU A 107 84.404 3.646 17.736 1.00 19.82 A ATOM 263 CA GLU A 107 84.294 5.086 17.903 1.00 21.14 A ATOM 264 CB GLU A 107 85.656 5.746 17.777 1.00 21.88 A ATOM 265 CG GLU A 107 86.562 5.428 18.926 1.00 26.09 A ATOM 266 CD GLU A 107 87.916 6.043 18.746 1.00 30.29 A ATOM 267 OE1 GLU A 107 88.212 7.057 19.434 1.00 32.48 A ATOM 268 OE2 GLU A 107 88.678 5.512 17.901 1.00 31.98 A ATOM 269 C GLU A 107 83.358 5.693 16.870 1.00 20.50 A ATOM 270 O GLU A 107 83.474 5.429 15.676 1.00 20.70 A ATOM 271 N TYR A 108 82.415 6.498 17.347 1.00 20.38 A ATOM 272 CA TYR A 108 81.464 7.172 16.477 1.00 18.49 A ATOM 273 CB TYR A 108 80.049 6.660 16.700 1.00 17.92 A ATOM 274 CG TYR A 108 79.828 5.247 16.238 1.00 23.37 A ATOM 275 CD1 TYR A 108 79.598 4.964 14.886 1.00 22.79 A ATOM 276 CE1 TYR A 108 79.357 3.648 14.458 1.00 23.56 A ATOM 277 CD2 TYR A 108 79.820 4.180 17.154 1.00 21.34 A ATOM 278 CE2 TYR A 108 79.583 2.873 16.740 1.00 20.43 A ATOM 279 CZ TYR A 108 79.346 2.609 15.392 1.00 23.44 A ATOM 280 OH TYR A 108 79.061 1.321 14.972 1.00 24.10 A ATOM 281 C TYR A 108 81.478 8.635 16.828 1.00 18.53 A ATOM 282 O TYR A 108 81.778 9.011 17.971 1.00 17.37 A ATOM 283 N ALA A 109 81.169 9.453 15.829 1.00 17.24 A ATOM 284 CA ALA A 109 81.053 10.885 16.006 1.00 15.98 A ATOM 285 CB ALA A 109 81.597 11.600 14.788 1.00 15.20 A ATOM 286 C ALA A 109 79.528 11.087 16.140 1.00 15.73 A ATOM 287 O ALA A 109 78.767 10.873 15.191 1.00 15.79 A ATOM 288 N ILE A 110 79.070 11.474 17.320 1.00 14.95 A ATOM 289 CA ILE A 110 77.636 11.636 17.511 1.00 15.99 A ATOM 290 CB ILE A 110 77.188 10.940 18.815 1.00 15.51 A ATOM 291 CG2 ILE A 110 75.697 11.126 19.039 1.00 14.44 A ATOM 292 CG1 ILE A 110 77.541 9.452 18.729 1.00 16.63 A ATOM 293 CD1 ILE A 110 76.964 8.595 19.847 1.00 16.83 A ATOM 294 C ILE A 110 77.176 13.085 17.514 1.00 16.55 A ATOM 295 O ILE A 110 77.583 13.873 18.370 1.00 16.24 A ATOM 296 N LYS A 111 76.343 13.430 16.538 1.00 16.03 A ATOM 297 CA LYS A 111 75.804 14.777 16.430 1.00 18.21 A ATOM 298 CB LYS A 111 75.341 15.065 14.997 1.00 19.36 A ATOM 299 CG LYS A 111 75.035 16.548 14.768 1.00 22.68 A ATOM 300 CD LYS A 111 74.461 16.844 13.396 1.00 23.67 A ATOM 301 CE LYS A 111 74.876 18.222 12.930 1.00 23.18 A ATOM 302 NZ LYS A 111 73.744 18.938 12.304 1.00 28.83 A ATOM 303 C LYS A 111 74.608 14.866 17.383 1.00 17.40 A ATOM 304 O LYS A 111 73.646 14.115 17.239 1.00 18.27 A ATOM 305 N ILE A 112 74.672 15.781 18.344 1.00 15.41 A ATOM 306 CA ILE A 112 73.609 15.938 19.331 1.00 16.56 A ATOM 307 CB ILE A 112 74.194 15.819 20.777 1.00 17.09 A ATOM 308 CG2 ILE A 112 73.073 15.926 21.830 1.00 11.60 A ATOM 309 CG1 ILE A 112 74.957 14.480 20.885 1.00 16.81 A ATOM 310 CD1 ILE A 112 75.771 14.262 22.178 1.00 15.96 A ATOM 311 C ILE A 112 72.876 17.261 19.158 1.00 17.98 A ATOM 312 O ILE A 112 73.504 18.314 18.965 1.00 16.70 A ATOM 313 N LEU A 113 71.546 17.198 19.195 1.00 19.61 A ATOM 314 CA LEU A 113 70.711 18.393 19.034 1.00 21.99 A ATOM 315 CB LEU A 113 70.058 18.434 17.641 1.00 22.17 A ATOM 316 CG LEU A 113 70.906 18.273 16.367 1.00 22.83 A ATOM 317 CD1 LEU A 113 71.124 16.792 16.059 1.00 22.72 A ATOM 318 CD2 LEU A 113 70.191 18.912 15.206 1.00 21.97 A ATOM 319 C LEU A 113 69.612 18.419 20.088 1.00 24.22 A ATOM 320 O LEU A 113 69.062 17.378 20.469 1.00 24.61 A ATOM 321 N GLU A 114 69.285 19.615 20.559 1.00 27.06 A ATOM 322 CA GLU A 114 68.247 19.759 21.567 1.00 28.93 A ATOM 323 CB GLU A 114 68.586 20.926 22.488 1.00 31.39 A ATOM 324 CG GLU A 114 67.671 21.026 23.684 1.00 39.92 A ATOM 325 CD GLU A 114 67.676 22.406 24.300 1.00 45.42 A ATOM 326 OE1 GLU A 114 67.160 23.356 23.655 1.00 46.90 A ATOM 327 OE2 GLU A 114 68.204 22.540 25.429 1.00 50.09 A ATOM 328 C GLU A 114 66.887 19.978 20.892 1.00 29.21 A ATOM 329 O GLU A 114 66.679 20.969 20.177 1.00 29.53 A ATOM 330 N LYS A 115 65.962 19.051 21.116 1.00 28.74 A ATOM 331 CA LYS A 115 64.642 19.152 20.507 1.00 29.44 A ATOM 332 CB LYS A 115 63.744 18.002 20.987 1.00 28.12 A ATOM 333 CG LYS A 115 63.827 16.758 20.103 1.00 28.47 A ATOM 334 CD LYS A 115 63.026 15.571 20.639 1.00 27.07 A ATOM 335 CE LYS A 115 63.738 14.854 21.779 1.00 28.88 A ATOM 336 NZ LYS A 115 62.963 13.672 22.282 1.00 26.42 A ATOM 337 C LYS A 115 63.947 20.502 20.724 1.00 29.72 A ATOM 338 O LYS A 115 63.310 21.025 19.799 1.00 30.03 A ATOM 339 N ALA A 116 64.082 21.091 21.910 1.00 28.83 A ATOM 340 CA ALA A 116 63.407 22.365 22.159 1.00 29.91 A ATOM 341 CB ALA A 116 63.470 22.749 23.647 1.00 28.16 A ATOM 342 C ALA A 116 63.976 23.480 21.311 1.00 30.93 A ATOM 343 O ALA A 116 63.231 24.217 20.667 1.00 32.28 A ATOM 344 N HIS A 117 65.297 23.593 21.292 1.00 31.66 A ATOM 345 CA HIS A 117 65.951 24.645 20.523 1.00 32.13 A ATOM 346 CB HIS A 117 67.472 24.571 20.728 1.00 34.12 A ATOM 347 CG HIS A 117 68.219 25.741 20.169 1.00 37.74 A ATOM 348 CD2 HIS A 117 67.794 26.959 19.761 1.00 39.67 A ATOM 349 ND1 HIS A 117 69.582 25.727 19.966 1.00 42.04 A ATOM 350 CE1 HIS A 117 69.965 26.884 19.454 1.00 41.07 A ATOM 351 NE2 HIS A 117 68.899 27.649 19.320 1.00 40.56 A ATOM 352 C HIS A 117 65.600 24.547 19.040 1.00 31.36 A ATOM 353 O HIS A 117 65.466 25.560 18.350 1.00 32.37 A ATOM 354 N ILE A 118 65.430 23.330 18.544 1.00 30.26 A ATOM 355 CA ILE A 118 65.102 23.158 17.132 1.00 29.28 A ATOM 356 CB ILE A 118 65.266 21.696 16.712 1.00 27.64 A ATOM 357 CG2 ILE A 118 64.560 21.439 15.401 1.00 22.46 A ATOM 358 CG1 ILE A 118 66.756 21.371 16.642 1.00 27.22 A ATOM 359 CD1 ILE A 118 67.036 19.917 16.437 1.00 30.51 A ATOM 360 C ILE A 118 63.688 23.618 16.816 1.00 30.41 A ATOM 361 O ILE A 118 63.444 24.251 15.785 1.00 29.55 A ATOM 362 N ILE A 119 62.756 23.291 17.705 1.00 29.59 A ATOM 363 CA ILE A 119 61.376 23.682 17.497 1.00 29.18 A ATOM 364 CB ILE A 119 60.447 22.979 18.506 1.00 27.15 A ATOM 365 CG2 ILE A 119 59.071 23.623 18.486 1.00 22.69 A ATOM 366 CG1 ILE A 119 60.394 21.486 18.173 1.00 23.45 A ATOM 367 CD1 ILE A 119 59.666 20.665 19.173 1.00 19.08 A ATOM 368 C ILE A 119 61.223 25.194 17.617 1.00 30.65 A ATOM 369 O ILE A 119 60.574 25.832 16.786 1.00 30.59 A ATOM 370 N ALA A 120 61.837 25.768 18.642 1.00 31.95 A ATOM 371 CA ALA A 120 61.752 27.205 18.848 1.00 33.69 A ATOM 372 CB ALA A 120 62.473 27.608 20.150 1.00 33.17 A ATOM 373 C ALA A 120 62.330 27.973 17.671 1.00 34.80 A ATOM 374 O ALA A 120 61.865 29.067 17.362 1.00 37.34 A ATOM 375 N GLU A 121 63.328 27.413 16.997 1.00 35.09 A ATOM 376 CA GLU A 121 63.941 28.116 15.872 1.00 35.31 A ATOM 377 CB GLU A 121 65.453 27.927 15.933 1.00 39.72 A ATOM 378 CG GLU A 121 66.103 28.735 17.038 1.00 45.91 A ATOM 379 CD GLU A 121 65.955 30.225 16.784 1.00 49.51 A ATOM 380 OE1 GLU A 121 66.634 30.736 15.866 1.00 52.87 A ATOM 381 OE2 GLU A 121 65.148 30.879 17.482 1.00 51.35 A ATOM 382 C GLU A 121 63.421 27.699 14.499 1.00 34.14 A ATOM 383 O GLU A 121 63.964 28.109 13.468 1.00 31.41 A ATOM 384 N ASN A 122 62.363 26.891 14.497 1.00 33.86 A ATOM 385 CA ASN A 122 61.771 26.367 13.266 1.00 34.00 A ATOM 386 CB ASN A 122 61.112 27.473 12.464 1.00 36.75 A ATOM 387 CG ASN A 122 59.962 28.081 13.193 1.00 39.62 A ATOM 388 OD1 ASN A 122 60.148 28.788 14.185 1.00 39.90 A ATOM 389 ND2 ASN A 122 58.753 27.794 12.727 1.00 41.02 A ATOM 390 C ASN A 122 62.798 25.686 12.397 1.00 31.78 A ATOM 391 O ASN A 122 62.958 26.035 11.230 1.00 32.05 A ATOM 392 N LYS A 123 63.494 24.714 12.965 1.00 28.71 A ATOM 393 CA LYS A 123 64.508 24.008 12.217 1.00 29.39 A ATOM 394 CB LYS A 123 65.842 24.036 12.974 1.00 31.70 A ATOM 395 CG LYS A 123 66.434 25.416 13.132 1.00 33.49 A ATOM 396 CD LYS A 123 66.612 26.076 11.763 1.00 37.43 A ATOM 397 CE LYS A 123 67.174 27.491 11.898 1.00 38.52 A ATOM 398 NZ LYS A 123 67.337 28.176 10.582 1.00 37.85 A ATOM 399 C LYS A 123 64.116 22.572 11.931 1.00 28.30 A ATOM 400 O LYS A 123 64.867 21.844 11.289 1.00 29.68 A ATOM 401 N VAL A 124 62.944 22.162 12.404 1.00 26.80 A ATOM 402 CA VAL A 124 62.484 20.796 12.175 1.00 26.73 A ATOM 403 CB VAL A 124 61.024 20.593 12.622 1.00 26.31 A ATOM 404 CG1 VAL A 124 60.532 19.222 12.191 1.00 25.31 A ATOM 405 CG2 VAL A 124 60.918 20.720 14.134 1.00 26.73 A ATOM 406 C VAL A 124 62.594 20.351 10.722 1.00 27.11 A ATOM 407 O VAL A 124 62.973 19.218 10.450 1.00 29.79 A ATOM 408 N PRO A 125 62.270 21.228 9.763 1.00 27.28 A ATOM 409 CD PRO A 125 61.610 22.544 9.818 1.00 27.49 A ATOM 410 CA PRO A 125 62.386 20.758 8.378 1.00 27.41 A ATOM 411 CB PRO A 125 61.775 21.904 7.563 1.00 26.08 A ATOM 412 CG PRO A 125 60.821 22.546 8.524 1.00 27.54 A ATOM 413 C PRO A 125 63.837 20.506 8.006 1.00 27.90 A ATOM 414 O PRO A 125 64.162 19.572 7.260 1.00 26.27 A ATOM 415 N TYR A 126 64.703 21.350 8.550 1.00 28.64 A ATOM 416 CA TYR A 126 66.123 21.271 8.288 1.00 30.11 A ATOM 417 CB TYR A 126 66.791 22.528 8.809 1.00 36.70 A ATOM 418 CG TYR A 126 66.440 23.774 8.013 1.00 44.64 A ATOM 419 CD1 TYR A 126 66.984 23.988 6.744 1.00 47.43 A ATOM 420 CE1 TYR A 126 66.737 25.173 6.037 1.00 50.16 A ATOM 421 CD2 TYR A 126 65.620 24.774 8.557 1.00 47.03 A ATOM 422 CE2 TYR A 126 65.369 25.955 7.861 1.00 49.52 A ATOM 423 CZ TYR A 126 65.936 26.152 6.605 1.00 50.60 A ATOM 424 OH TYR A 126 65.754 27.349 5.941 1.00 52.77 A ATOM 425 C TYR A 126 66.794 20.041 8.874 1.00 28.69 A ATOM 426 O TYR A 126 67.613 19.407 8.208 1.00 28.32 A ATOM 427 N VAL A 127 66.464 19.714 10.118 1.00 25.64 A ATOM 428 CA VAL A 127 67.033 18.550 10.766 1.00 24.89 A ATOM 429 CB VAL A 127 66.664 18.513 12.258 1.00 26.70 A ATOM 430 CG1 VAL A 127 67.158 17.206 12.881 1.00 22.51 A ATOM 431 CG2 VAL A 127 67.255 19.743 12.972 1.00 23.84 A ATOM 432 C VAL A 127 66.521 17.276 10.097 1.00 24.81 A ATOM 433 O VAL A 127 67.260 16.315 9.890 1.00 24.02 A ATOM 434 N THR A 128 65.245 17.290 9.755 1.00 24.02 A ATOM 435 CA THR A 128 64.608 16.164 9.088 1.00 24.59 A ATOM 436 CB THR A 128 63.123 16.471 8.843 1.00 25.38 A ATOM 437 CG1 THR A 128 62.478 16.652 10.106 1.00 25.76 A ATOM 438 CG2 THR A 128 62.451 15.354 8.066 1.00 22.88 A ATOM 439 C THR A 128 65.266 15.875 7.744 1.00 24.53 A ATOM 440 O THR A 128 65.560 14.729 7.426 1.00 25.53 A ATOM 441 N ARG A 129 65.477 16.925 6.957 1.00 24.82 A ATOM 442 CA ARG A 129 66.099 16.812 5.646 1.00 25.49 A ATOM 443 CB ARG A 129 66.111 18.181 4.959 1.00 26.78 A ATOM 444 CG ARG A 129 66.648 18.175 3.529 1.00 32.33 A ATOM 445 CD ARG A 129 66.579 19.563 2.878 1.00 36.93 A ATOM 446 NE ARG A 129 65.326 20.249 3.184 1.00 42.70 A ATOM 447 CZ ARG A 129 65.254 21.462 3.730 1.00 46.67 A ATOM 448 NH1 ARG A 129 66.366 22.128 4.018 1.00 48.50 A ATOM 449 NH2 ARG A 129 64.073 21.997 4.027 1.00 48.90 A ATOM 450 C ARG A 129 67.532 16.296 5.801 1.00 26.46 A ATOM 451 O ARG A 129 68.002 15.456 5.020 1.00 24.76 A ATOM 452 N GLU A 130 68.216 16.795 6.825 1.00 25.56 A ATOM 453 CA GLU A 130 69.582 16.393 7.076 1.00 28.29 A ATOM 454 CB GLU A 130 70.118 17.106 8.310 1.00 27.95 A ATOM 455 CG GLU A 130 71.591 16.875 8.539 1.00 29.48 A ATOM 456 CD GLU A 130 72.107 17.566 9.787 1.00 32.14 A ATOM 457 OE1 GLU A 130 71.297 18.221 10.483 1.00 32.67 A ATOM 458 OE2 GLU A 130 73.325 17.450 10.069 1.00 32.21 A ATOM 459 C GLU A 130 69.665 14.886 7.279 1.00 29.86 A ATOM 460 O GLU A 130 70.498 14.200 6.668 1.00 29.35 A ATOM 461 N ARG A 131 68.797 14.382 8.150 1.00 30.84 A ATOM 462 CA ARG A 131 68.763 12.966 8.451 1.00 31.62 A ATOM 463 CB ARG A 131 67.786 12.684 9.598 1.00 33.12 A ATOM 464 CG ARG A 131 67.557 11.190 9.831 1.00 36.17 A ATOM 465 CD ARG A 131 66.560 10.925 10.946 1.00 41.69 A ATOM 466 NE ARG A 131 66.330 9.492 11.166 1.00 46.62 A ATOM 467 CZ ARG A 131 65.692 8.986 12.224 1.00 48.29 A ATOM 468 NH1 ARG A 131 65.215 9.795 13.165 1.00 49.51 A ATOM 469 NH2 ARG A 131 65.544 7.671 12.352 1.00 48.76 A ATOM 470 C ARG A 131 68.371 12.138 7.235 1.00 30.59 A ATOM 471 O ARG A 131 68.897 11.051 7.026 1.00 29.96 A ATOM 472 N ASP A 132 67.446 12.649 6.433 1.00 29.54 A ATOM 473 CA ASP A 132 67.000 11.913 5.259 1.00 29.40 A ATOM 474 CB ASP A 132 65.735 12.565 4.708 1.00 32.43 A ATOM 475 CG ASP A 132 64.531 12.395 5.655 1.00 38.15 A ATOM 476 OD1 ASP A 132 64.749 12.227 6.881 1.00 40.40 A ATOM 477 OD2 ASP A 132 63.365 12.439 5.186 1.00 41.19 A ATOM 478 C ASP A 132 68.088 11.789 4.189 1.00 27.62 A ATOM 479 O ASP A 132 68.232 10.744 3.553 1.00 26.54 A ATOM 480 N VAL A 133 68.862 12.850 4.011 1.00 25.14 A ATOM 481 CA VAL A 133 69.939 12.857 3.044 1.00 24.12 A ATOM 482 CB VAL A 133 70.451 14.272 2.833 1.00 24.07 A ATOM 483 CG1 VAL A 133 71.802 14.247 2.143 1.00 23.77 A ATOM 484 CG2 VAL A 133 69.461 15.030 2.008 1.00 24.30 A ATOM 485 C VAL A 133 71.099 11.975 3.504 1.00 24.97 A ATOM 486 O VAL A 133 71.672 11.221 2.712 1.00 24.95 A ATOM 487 N MET A 134 71.458 12.074 4.779 1.00 23.41 A ATOM 488 CA MET A 134 72.539 11.255 5.268 1.00 23.12 A ATOM 489 CB MET A 134 72.932 11.653 6.683 1.00 21.12 A ATOM 490 CG MET A 134 73.608 13.005 6.759 1.00 21.21 A ATOM 491 SD MET A 134 74.530 13.204 8.291 1.00 20.52 A ATOM 492 CE MET A 134 73.172 13.347 9.534 1.00 17.71 A ATOM 493 C MET A 134 72.163 9.783 5.237 1.00 24.75 A ATOM 494 O MET A 134 73.027 8.918 5.039 1.00 25.73 A ATOM 495 N SER A 135 70.885 9.474 5.425 1.00 23.96 A ATOM 496 CA SER A 135 70.484 8.064 5.408 1.00 24.82 A ATOM 497 CB SER A 135 69.048 7.889 5.917 1.00 24.63 A ATOM 498 OG SER A 135 68.139 8.496 5.015 1.00 29.80 A ATOM 499 C SER A 135 70.585 7.479 4.003 1.00 22.35 A ATOM 500 O SER A 135 70.534 6.274 3.829 1.00 21.60 A ATOM 501 N ARG A 136 70.729 8.335 3.004 1.00 21.91 A ATOM 502 CA ARG A 136 70.815 7.858 1.631 1.00 23.76 A ATOM 503 CB ARG A 136 69.988 8.762 0.714 1.00 25.55 A ATOM 504 CG ARG A 136 68.500 8.782 1.069 1.00 31.38 A ATOM 505 CD ARG A 136 67.764 9.897 0.332 1.00 33.65 A ATOM 506 NE ARG A 136 68.024 9.809 −1.099 1.00 38.77 A ATOM 507 CZ ARG A 136 67.654 10.718 −1.996 1.00 41.27 A ATOM 508 NH1 ARG A 136 66.988 11.806 −1.604 1.00 42.53 A ATOM 509 NH2 ARG A 136 67.971 10.544 −3.286 1.00 39.41 A ATOM 510 C ARG A 136 72.248 7.789 1.131 1.00 22.64 A ATOM 511 O ARG A 136 72.520 7.268 0.052 1.00 22.43 A ATOM 512 N LEU A 137 73.168 8.318 1.919 1.00 22.66 A ATOM 513 CA LEU A 137 74.568 8.307 1.535 1.00 22.60 A ATOM 514 CB LEU A 137 75.348 9.375 2.308 1.00 20.28 A ATOM 515 CG LEU A 137 74.842 10.793 2.068 1.00 19.72 A ATOM 516 CD1 LEU A 137 75.695 11.816 2.840 1.00 17.83 A ATOM 517 CD2 LEU A 137 74.855 11.062 0.564 1.00 18.39 A ATOM 518 C LEU A 137 75.195 6.950 1.775 1.00 22.60 A ATOM 519 O LEU A 137 75.203 6.445 2.892 1.00 23.75 A ATOM 520 N ASP A 138 75.723 6.371 0.710 1.00 22.09 A ATOM 521 CA ASP A 138 76.383 5.083 0.788 1.00 22.63 A ATOM 522 CB ASP A 138 75.419 3.988 0.340 1.00 25.16 A ATOM 523 CG ASP A 138 75.976 2.622 0.582 1.00 26.26 A ATOM 524 OD1 ASP A 138 76.658 2.480 1.611 1.00 27.29 A ATOM 525 OD2 ASP A 138 75.740 1.708 −0.237 1.00 30.75 A ATOM 526 C ASP A 138 77.617 5.112 −0.124 1.00 20.82 A ATOM 527 O ASP A 138 77.656 4.445 −1.155 1.00 22.94 A ATOM 528 N HIS A 139 78.612 5.902 0.250 1.00 16.77 A ATOM 529 CA HIS A 139 79.813 6.050 −0.557 1.00 16.21 A ATOM 530 CB HIS A 139 79.614 7.180 −1.583 1.00 15.30 A ATOM 531 CG HIS A 139 80.755 7.348 −2.534 1.00 16.37 A ATOM 532 CD2 HIS A 139 80.853 7.087 −3.860 1.00 15.32 A ATOM 533 ND1 HIS A 139 81.998 7.802 −2.139 1.00 17.12 A ATOM 534 CE1 HIS A 139 82.811 7.810 −3.184 1.00 15.92 A ATOM 535 NE2 HIS A 139 82.140 7.380 −4.238 1.00 13.96 A ATOM 536 C HIS A 139 80.985 6.371 0.357 1.00 16.70 A ATOM 537 O HIS A 139 80.848 7.116 1.317 1.00 16.89 A ATOM 538 N PRO A 140 82.164 5.823 0.056 1.00 16.94 A ATOM 539 CD PRO A 140 82.508 4.991 −1.108 1.00 17.10 A ATOM 540 CA PRO A 140 83.334 6.079 0.895 1.00 17.98 A ATOM 541 CB PRO A 140 84.390 5.163 0.291 1.00 17.03 A ATOM 542 CG PRO A 140 84.003 5.114 −1.159 1.00 18.59 A ATOM 543 C PRO A 140 83.822 7.528 1.070 1.00 18.59 A ATOM 544 O PRO A 140 84.528 7.817 2.021 1.00 20.11 A ATOM 545 N PHE A 141 83.460 8.444 0.179 1.00 19.62 A ATOM 546 CA PHE A 141 83.909 9.833 0.345 1.00 18.34 A ATOM 547 CB PHE A 141 84.223 10.474 −1.010 1.00 17.53 A ATOM 548 CG PHE A 141 85.440 9.880 −1.694 1.00 17.38 A ATOM 549 CD1 PHE A 141 86.450 9.275 −0.938 1.00 17.01 A ATOM 550 CD2 PHE A 141 85.579 9.926 −3.081 1.00 15.76 A ATOM 551 CE1 PHE A 141 87.572 8.724 −1.550 1.00 16.13 A ATOM 552 CE2 PHE A 141 86.707 9.375 −3.708 1.00 16.99 A ATOM 553 CZ PHE A 141 87.705 8.772 −2.938 1.00 15.01 A ATOM 554 C PHE A 141 82.893 10.680 1.095 1.00 18.14 A ATOM 555 O PHE A 141 83.012 11.896 1.144 1.00 20.74 A ATOM 556 N PHE A 142 81.901 10.037 1.697 1.00 15.85 A ATOM 557 CA PHE A 142 80.887 10.761 2.444 1.00 15.95 A ATOM 558 CB PHE A 142 79.558 10.757 1.690 1.00 15.20 A ATOM 559 CG PHE A 142 79.507 11.721 0.542 1.00 15.62 A ATOM 560 CD1 PHE A 142 79.295 13.086 0.768 1.00 14.51 A ATOM 561 CD2 PHE A 142 79.651 11.265 −0.771 1.00 12.05 A ATOM 562 CE1 PHE A 142 79.222 13.991 −0.291 1.00 13.97 A ATOM 563 CE2 PHE A 142 79.582 12.157 −1.840 1.00 15.46 A ATOM 564 CZ PHE A 142 79.365 13.536 −1.601 1.00 14.89 A ATOM 565 C PHE A 142 80.654 10.167 3.824 1.00 15.60 A ATOM 566 O PHE A 142 80.886 8.986 4.061 1.00 15.39 A ATOM 567 N VAL A 143 80.182 11.001 4.733 1.00 15.87 A ATOM 568 CA VAL A 143 79.878 10.564 6.075 1.00 15.04 A ATOM 569 CB VAL A 143 79.304 11.727 6.905 1.00 15.26 A ATOM 570 CG1 VAL A 143 78.012 12.231 6.276 1.00 11.03 A ATOM 571 CG2 VAL A 143 79.100 11.296 8.350 1.00 14.40 A ATOM 572 C VAL A 143 78.828 9.479 5.935 1.00 15.52 A ATOM 573 O VAL A 143 78.076 9.453 4.963 1.00 15.45 A ATOM 574 N LYS A 144 78.794 8.580 6.907 1.00 16.29 A ATOM 575 CA LYS A 144 77.848 7.482 6.933 1.00 17.45 A ATOM 576 CB LYS A 144 78.625 6.150 6.895 1.00 18.05 A ATOM 577 CG LYS A 144 77.963 4.967 7.596 1.00 24.34 A ATOM 578 CD LYS A 144 76.922 4.263 6.752 1.00 26.35 A ATOM 579 CE LYS A 144 77.461 2.926 6.213 1.00 30.22 A ATOM 580 NZ LYS A 144 77.576 1.882 7.271 1.00 28.27 A ATOM 581 C LYS A 144 77.024 7.626 8.222 1.00 17.39 A ATOM 582 O LYS A 144 77.565 7.913 9.284 1.00 16.92 A ATOM 583 N LEU A 145 75.711 7.458 8.116 1.00 17.41 A ATOM 584 CA LEU A 145 74.836 7.549 9.274 1.00 18.13 A ATOM 585 CB LEU A 145 73.514 8.210 8.893 1.00 18.86 A ATOM 586 CG LEU A 145 72.612 8.850 9.964 1.00 20.13 A ATOM 587 CD1 LEU A 145 71.157 8.607 9.582 1.00 19.48 A ATOM 588 CD2 LEU A 145 72.900 8.311 11.331 1.00 17.86 A ATOM 589 C LEU A 145 74.559 6.113 9.689 1.00 18.85 A ATOM 590 O LEU A 145 73.905 5.379 8.954 1.00 20.15 A ATOM 591 N TYR A 146 75.030 5.713 10.867 1.00 18.09 A ATOM 592 CA TYR A 146 74.830 4.341 11.329 1.00 15.93 A ATOM 593 CB TYR A 146 76.013 3.871 12.154 1.00 14.52 A ATOM 594 CG TYR A 146 77.295 3.776 11.390 1.00 13.98 A ATOM 595 CD1 TYR A 146 78.093 4.907 11.193 1.00 15.01 A ATOM 596 CE1 TYR A 146 79.329 4.815 10.548 1.00 14.94 A ATOM 597 CD2 TYR A 146 77.752 2.541 10.912 1.00 14.36 A ATOM 598 CE2 TYR A 146 78.984 2.426 10.266 1.00 15.47 A ATOM 599 CZ TYR A 146 79.770 3.566 10.090 1.00 15.70 A ATOM 600 OH TYR A 146 80.999 3.473 9.491 1.00 16.29 A ATOM 601 C TYR A 146 73.591 4.135 12.154 1.00 16.74 A ATOM 602 O TYR A 146 73.004 3.050 12.132 1.00 17.63 A ATOM 603 N PHE A 147 73.198 5.158 12.901 1.00 15.90 A ATOM 604 CA PHE A 147 72.012 5.041 13.745 1.00 17.10 A ATOM 605 CB PHE A 147 72.265 4.057 14.932 1.00 14.80 A ATOM 606 CG PHE A 147 73.509 4.366 15.747 1.00 16.36 A ATOM 607 CD1 PHE A 147 73.526 5.427 16.657 1.00 15.38 A ATOM 608 CD2 PHE A 147 74.701 3.663 15.514 1.00 16.83 A ATOM 609 CE1 PHE A 147 74.709 5.801 17.314 1.00 15.96 A ATOM 610 CE2 PHE A 147 75.907 4.024 16.163 1.00 16.65 A ATOM 611 CZ PHE A 147 75.908 5.107 17.069 1.00 16.96 A ATOM 612 C PHE A 147 71.550 6.378 14.286 1.00 17.73 A ATOM 613 O PHE A 147 72.225 7.399 14.145 1.00 18.47 A ATOM 614 N THR A 148 70.376 6.352 14.897 1.00 19.28 A ATOM 615 CA THR A 148 69.801 7.529 15.532 1.00 19.50 A ATOM 616 CB THR A 148 68.846 8.308 14.597 1.00 19.24 A ATOM 617 OG1 THR A 148 67.722 7.485 14.271 1.00 18.29 A ATOM 618 CG2 THR A 148 69.563 8.727 13.311 1.00 18.53 A ATOM 619 C THR A 148 68.976 7.071 16.718 1.00 19.68 A ATOM 620 O THR A 148 68.556 5.915 16.802 1.00 20.20 A ATOM 621 N PHE A 149 68.765 7.975 17.653 1.00 20.20 A ATOM 622 CA PHE A 149 67.926 7.687 18.797 1.00 20.34 A ATOM 623 CB PHE A 149 68.558 6.626 19.728 1.00 19.06 A ATOM 624 CG PHE A 149 69.932 6.961 20.216 1.00 18.27 A ATOM 625 CD1 PHE A 149 70.114 7.745 21.357 1.00 19.90 A ATOM 626 CD2 PHE A 149 71.049 6.467 19.559 1.00 19.21 A ATOM 627 CE1 PHE A 149 71.387 8.028 21.840 1.00 19.04 A ATOM 628 CE2 PHE A 149 72.341 6.741 20.025 1.00 19.95 A ATOM 629 CZ PHE A 149 72.513 7.520 21.167 1.00 21.19 A ATOM 630 C PHE A 149 67.693 9.004 19.487 1.00 20.94 A ATOM 631 O PHE A 149 68.192 10.035 19.042 1.00 17.91 A ATOM 632 N GLN A 150 66.888 8.988 20.539 1.00 25.44 A ATOM 633 CA GLN A 150 66.609 10.212 21.279 1.00 29.09 A ATOM 634 CB GLN A 150 65.518 11.039 20.571 1.00 29.07 A ATOM 635 CG GLN A 150 64.194 10.322 20.309 1.00 31.07 A ATOM 636 CD GLN A 150 63.150 11.227 19.609 1.00 32.52 A ATOM 637 OE1 GLN A 150 62.503 12.075 20.243 1.00 30.50 A ATOM 638 NE2 GLN A 150 63.009 11.056 18.294 1.00 29.34 A ATOM 639 C GLN A 150 66.190 9.927 22.707 1.00 29.59 A ATOM 640 O GLN A 150 65.738 8.832 23.018 1.00 30.34 A ATOM 641 N ASP A 151 66.407 10.892 23.590 1.00 31.52 A ATOM 642 CA ASP A 151 65.957 10.750 24.967 1.00 32.22 A ATOM 643 CB ASP A 151 67.093 10.948 25.974 1.00 31.30 A ATOM 644 CG ASP A 151 67.832 12.246 25.790 1.00 32.39 A ATOM 645 OD1 ASP A 151 67.241 13.217 25.263 1.00 34.30 A ATOM 646 OD2 ASP A 151 69.011 12.290 26.195 1.00 32.02 A ATOM 647 C ASP A 151 64.914 11.858 25.063 1.00 33.56 A ATOM 648 O ASP A 151 64.495 12.387 24.033 1.00 34.76 A ATOM 649 N ASP A 152 64.498 12.239 26.261 1.00 35.00 A ATOM 650 CA ASP A 152 63.462 13.268 26.369 1.00 36.72 A ATOM 651 CB ASP A 152 63.053 13.465 27.830 1.00 38.27 A ATOM 652 CG ASP A 152 62.237 12.312 28.351 1.00 42.45 A ATOM 653 OD1 ASP A 152 61.377 11.824 27.579 1.00 43.52 A ATOM 654 OD2 ASP A 152 62.444 11.900 29.519 1.00 44.28 A ATOM 655 C ASP A 152 63.758 14.627 25.759 1.00 36.47 A ATOM 656 O ASP A 152 62.857 15.289 25.242 1.00 36.12 A ATOM 657 N GLU A 153 65.021 15.029 25.781 1.00 36.09 A ATOM 658 CA GLU A 153 65.358 16.343 25.292 1.00 35.16 A ATOM 659 CB GLU A 153 65.976 17.137 26.442 1.00 39.45 A ATOM 660 CG GLU A 153 65.486 16.714 27.830 1.00 45.94 A ATOM 661 CD GLU A 153 66.383 15.652 28.468 1.00 51.78 A ATOM 662 OE1 GLU A 153 67.563 15.977 28.746 1.00 54.51 A ATOM 663 OE2 GLU A 153 65.924 14.500 28.689 1.00 52.47 A ATOM 664 C GLU A 153 66.258 16.455 24.073 1.00 32.91 A ATOM 665 O GLU A 153 66.304 17.524 23.457 1.00 31.19 A ATOM 666 N LYS A 154 66.959 15.376 23.710 1.00 30.19 A ATOM 667 CA LYS A 154 67.898 15.431 22.582 1.00 26.56 A ATOM 668 CB LYS A 154 69.323 15.414 23.121 1.00 24.92 A ATOM 669 CG LYS A 154 69.630 16.551 24.041 1.00 23.66 A ATOM 670 CD LYS A 154 70.944 16.355 24.750 1.00 20.95 A ATOM 671 CE LYS A 154 71.274 17.583 25.576 1.00 18.98 A ATOM 672 NZ LYS A 154 72.491 17.388 26.360 1.00 19.19 A ATOM 673 C LYS A 154 67.806 14.374 21.487 1.00 25.00 A ATOM 674 O LYS A 154 67.342 13.257 21.701 1.00 25.62 A ATOM 675 N LEU A 155 68.276 14.759 20.308 1.00 23.36 A ATOM 676 CA LEU A 155 68.337 13.881 19.140 1.00 22.19 A ATOM 677 CB LEU A 155 67.946 14.624 17.864 1.00 21.64 A ATOM 678 CG LEU A 155 66.539 15.167 17.707 1.00 22.58 A ATOM 679 CD1 LEU A 155 66.437 15.847 16.350 1.00 22.74 A ATOM 680 CD2 LEU A 155 65.533 14.034 17.815 1.00 23.23 A ATOM 681 C LEU A 155 69.798 13.474 19.004 1.00 20.69 A ATOM 682 O LEU A 155 70.693 14.287 19.249 1.00 21.61 A ATOM 683 N TYR A 156 70.036 12.238 18.592 1.00 18.69 A ATOM 684 CA TYR A 156 71.393 11.737 18.431 1.00 18.65 A ATOM 685 CB TYR A 156 71.690 10.661 19.489 1.00 18.51 A ATOM 686 CG TYR A 156 71.602 11.148 20.913 1.00 17.86 A ATOM 687 CD1 TYR A 156 70.372 11.287 21.550 1.00 18.38 A ATOM 688 CE1 TYR A 156 70.286 11.752 22.862 1.00 18.95 A ATOM 689 CD2 TYR A 156 72.755 11.488 21.621 1.00 19.32 A ATOM 690 CE2 TYR A 156 72.690 11.957 22.942 1.00 18.14 A ATOM 691 CZ TYR A 156 71.449 12.086 23.551 1.00 18.56 A ATOM 692 OH TYR A 156 71.372 12.547 24.838 1.00 18.33 A ATOM 693 C TYR A 156 71.640 11.125 17.059 1.00 18.03 A ATOM 694 O TYR A 156 70.903 10.250 16.646 1.00 18.18 A ATOM 695 N PHE A 157 72.662 11.568 16.338 1.00 17.19 A ATOM 696 CA PHE A 157 72.937 10.934 15.062 1.00 17.15 A ATOM 697 CB PHE A 157 72.980 11.951 13.918 1.00 21.54 A ATOM 698 CG PHE A 157 71.663 12.638 13.651 1.00 26.82 A ATOM 699 CD1 PHE A 157 70.471 12.165 14.221 1.00 30.87 A ATOM 700 CD2 PHE A 157 71.617 13.794 12.869 1.00 28.42 A ATOM 701 CE1 PHE A 157 69.249 12.845 14.024 1.00 30.45 A ATOM 702 CE2 PHE A 157 70.407 14.483 12.661 1.00 29.44 A ATOM 703 CZ PHE A 157 69.224 14.008 13.243 1.00 30.41 A ATOM 704 C PHE A 157 74.286 10.244 15.184 1.00 16.38 A ATOM 705 O PHE A 157 75.256 10.883 15.527 1.00 17.91 A ATOM 706 N GLY A 158 74.347 8.942 14.919 1.00 16.20 A ATOM 707 CA GLY A 158 75.614 8.232 15.009 1.00 15.78 A ATOM 708 C GLY A 158 76.322 8.285 13.671 1.00 16.51 A ATOM 709 O GLY A 158 75.876 7.659 12.710 1.00 17.95 A ATOM 710 N LEU A 159 77.423 9.028 13.600 1.00 14.97 A ATOM 711 CA LEU A 159 78.143 9.177 12.342 1.00 15.17 A ATOM 712 CB LEU A 159 78.264 10.669 12.012 1.00 13.14 A ATOM 713 CG LEU A 159 76.989 11.518 12.133 1.00 12.95 A ATOM 714 CD1 LEU A 159 77.347 13.002 11.872 1.00  7.84 A ATOM 715 CD2 LEU A 159 75.926 11.020 11.138 1.00 11.24 A ATOM 716 C LEU A 159 79.535 8.540 12.300 1.00 15.49 A ATOM 717 O LEU A 159 80.136 8.256 13.333 1.00 15.76 A ATOM 718 N SER A 160 80.051 8.313 11.097 1.00 14.32 A ATOM 719 CA SER A 160 81.389 7.759 10.984 1.00 14.68 A ATOM 720 CB SER A 160 81.699 7.386 9.529 1.00 12.79 A ATOM 721 OG SER A 160 81.395 8.432 8.626 1.00 16.15 A ATOM 722 C SER A 160 82.365 8.823 11.509 1.00 15.82 A ATOM 723 O SER A 160 82.152 10.029 11.333 1.00 17.75 A ATOM 724 N TYR A 161 83.418 8.386 12.184 1.00 16.30 A ATOM 725 CA TYR A 161 84.399 9.309 12.740 1.00 17.11 A ATOM 726 CB TYR A 161 84.863 8.785 14.100 1.00 16.09 A ATOM 727 CG TYR A 161 86.020 9.529 14.717 1.00 19.80 A ATOM 728 CD1 TYR A 161 86.070 10.933 14.700 1.00 18.64 A ATOM 729 CE1 TYR A 161 87.091 11.625 15.345 1.00 19.50 A ATOM 730 CD2 TYR A 161 87.032 8.837 15.394 1.00 20.09 A ATOM 731 CE2 TYR A 161 88.057 9.517 16.047 1.00 21.66 A ATOM 732 CZ TYR A 161 88.085 10.918 16.022 1.00 23.52 A ATOM 733 OH TYR A 161 89.111 11.600 16.674 1.00 22.64 A ATOM 734 C TYR A 161 85.594 9.495 11.815 1.00 17.86 A ATOM 735 O TYR A 161 86.269 8.527 11.459 1.00 19.30 A ATOM 736 N ALA A 162 85.854 10.736 11.418 1.00 18.22 A ATOM 737 CA ALA A 162 86.990 11.040 10.546 1.00 19.59 A ATOM 738 CB ALA A 162 86.569 12.063 9.466 1.00 19.99 A ATOM 739 C ALA A 162 88.051 11.629 11.472 1.00 19.11 A ATOM 740 O ALA A 162 88.050 12.828 11.736 1.00 18.81 A ATOM 741 N ALA A 163 88.952 10.775 11.956 1.00 18.78 A ATOM 742 CA ALA A 163 89.994 11.165 12.918 1.00 18.84 A ATOM 743 CB ALA A 163 90.867 9.924 13.279 1.00 19.04 A ATOM 744 C ALA A 163 90.908 12.357 12.604 1.00 18.22 A ATOM 745 O ALA A 163 91.290 13.101 13.508 1.00 16.79 A ATOM 746 N ASN A 164 91.251 12.560 11.340 1.00 17.46 A ATOM 747 CA ASN A 164 92.148 13.645 11.023 1.00 17.79 A ATOM 748 CB ASN A 164 92.990 13.270 9.803 1.00 20.45 A ATOM 749 CG ASN A 164 93.919 12.092 10.097 1.00 21.08 A ATOM 750 OD1 ASN A 164 94.663 12.117 11.066 1.00 21.57 A ATOM 751 ND2 ASN A 164 93.862 11.059 9.271 1.00 24.54 A ATOM 752 C ASN A 164 91.555 15.044 10.889 1.00 18.34 A ATOM 753 O ASN A 164 92.293 16.005 10.634 1.00 19.83 A ATOM 754 N GLY A 165 90.247 15.176 11.083 1.00 15.01 A ATOM 755 CA GLY A 165 89.644 16.490 11.022 1.00 15.54 A ATOM 756 C GLY A 165 89.580 17.212 9.683 1.00 17.67 A ATOM 757 O GLY A 165 89.607 16.600 8.613 1.00 19.49 A ATOM 758 N GLU A 166 89.510 18.534 9.753 1.00 17.46 A ATOM 759 CA GLU A 166 89.378 19.379 8.577 1.00 19.26 A ATOM 760 CB GLU A 166 89.064 20.805 9.019 1.00 21.87 A ATOM 761 CG GLU A 166 88.057 20.917 10.149 1.00 24.70 A ATOM 762 CD GLU A 166 87.723 22.359 10.477 1.00 26.05 A ATOM 763 OE1 GLU A 166 88.469 23.251 10.001 1.00 25.93 A ATOM 764 OE2 GLU A 166 86.726 22.598 11.213 1.00 25.24 A ATOM 765 C GLU A 166 90.538 19.441 7.592 1.00 20.11 A ATOM 766 O GLU A 166 91.707 19.501 7.978 1.00 22.88 A ATOM 767 N LEU A 167 90.195 19.443 6.312 1.00 18.72 A ATOM 768 CA LEU A 167 91.173 19.565 5.242 1.00 17.38 A ATOM 769 CB LEU A 167 90.463 19.516 3.888 1.00 15.71 A ATOM 770 CG LEU A 167 91.238 19.817 2.601 1.00 15.42 A ATOM 771 CD1 LEU A 167 92.242 18.704 2.343 1.00 14.98 A ATOM 772 CD2 LEU A 167 90.265 19.947 1.416 1.00 12.32 A ATOM 773 C LEU A 167 91.817 20.940 5.438 1.00 19.75 A ATOM 774 O LEU A 167 93.030 21.103 5.266 1.00 19.61 A ATOM 775 N LEU A 168 91.001 21.928 5.812 1.00 20.53 A ATOM 776 CA LEU A 168 91.516 23.277 6.033 1.00 22.20 A ATOM 777 CB LEU A 168 90.436 24.192 6.637 1.00 20.41 A ATOM 778 CG LEU A 168 90.923 25.611 7.024 1.00 21.71 A ATOM 779 CD1 LEU A 168 91.275 26.413 5.768 1.00 20.09 A ATOM 780 CD2 LEU A 168 89.837 26.341 7.797 1.00 20.84 A ATOM 781 C LEU A 168 92.731 23.245 6.968 1.00 23.07 A ATOM 782 O LEU A 168 93.636 24.054 6.838 1.00 22.18 A ATOM 783 N LYS A 169 92.742 22.305 7.905 1.00 24.67 A ATOM 784 CA LYS A 169 93.844 22.192 8.850 1.00 28.56 A ATOM 785 CB LYS A 169 93.561 21.076 9.858 1.00 31.12 A ATOM 786 CG LYS A 169 94.615 20.933 10.938 1.00 35.60 A ATOM 787 CD LYS A 169 94.436 19.652 11.765 1.00 39.37 A ATOM 788 CE LYS A 169 94.832 18.410 10.961 1.00 42.26 A ATOM 789 NZ LYS A 169 94.664 17.131 11.725 1.00 42.83 A ATOM 790 C LYS A 169 95.151 21.902 8.119 1.00 29.24 A ATOM 791 O LYS A 169 96.190 22.505 8.398 1.00 30.32 A ATOM 792 N TYR A 170 95.101 20.970 7.179 1.00 29.12 A ATOM 793 CA TYR A 170 96.290 20.619 6.423 1.00 28.18 A ATOM 794 CB TYR A 170 96.037 19.344 5.637 1.00 25.30 A ATOM 795 CG TYR A 170 95.926 18.182 6.569 1.00 27.01 A ATOM 796 CD1 TYR A 170 97.072 17.533 7.053 1.00 26.92 A ATOM 797 CE1 TYR A 170 96.974 16.532 8.008 1.00 25.37 A ATOM 798 CD2 TYR A 170 94.688 17.792 7.062 1.00 25.14 A ATOM 799 CE2 TYR A 170 94.580 16.807 8.009 1.00 26.49 A ATOM 800 CZ TYR A 170 95.720 16.179 8.484 1.00 26.98 A ATOM 801 OH TYR A 170 95.580 15.223 9.456 1.00 27.66 A ATOM 802 C TYR A 170 96.690 21.742 5.507 1.00 28.69 A ATOM 803 O TYR A 170 97.875 21.971 5.285 1.00 30.98 A ATOM 804 N ILE A 171 95.705 22.452 4.976 1.00 28.95 A ATOM 805 CA ILE A 171 96.006 23.550 4.088 1.00 29.79 A ATOM 806 CB ILE A 171 94.721 24.233 3.579 1.00 29.29 A ATOM 807 CG2 ILE A 171 95.082 25.439 2.714 1.00 28.21 A ATOM 808 CG1 ILE A 171 93.906 23.227 2.747 1.00 29.66 A ATOM 809 CD1 ILE A 171 92.567 23.754 2.224 1.00 29.13 A ATOM 810 C ILE A 171 96.897 24.536 4.833 1.00 31.13 A ATOM 811 O ILE A 171 97.925 24.956 4.300 1.00 30.93 A ATOM 812 N ARG A 172 96.525 24.862 6.075 1.00 32.00 A ATOM 813 CA ARG A 172 97.294 25.789 6.903 1.00 32.60 A ATOM 814 CB ARG A 172 96.527 26.175 8.163 1.00 32.77 A ATOM 815 CG ARG A 172 95.257 26.982 7.972 1.00 38.24 A ATOM 816 CD ARG A 172 94.853 27.602 9.335 1.00 43.47 A ATOM 817 NE ARG A 172 93.501 28.181 9.412 1.00 46.65 A ATOM 818 CZ ARG A 172 92.903 28.888 8.448 1.00 47.62 A ATOM 819 NH1 ARG A 172 93.517 29.115 7.287 1.00 47.16 A ATOM 820 NH2 ARG A 172 91.691 29.398 8.659 1.00 45.61 A ATOM 821 C ARG A 172 98.646 25.219 7.338 1.00 32.95 A ATOM 822 O ARG A 172 99.644 25.920 7.311 1.00 34.27 A ATOM 823 N ALA A 173 98.674 23.960 7.761 1.00 32.74 A ATOM 824 CA ALA A 173 99.912 23.341 8.209 1.00 32.81 A ATOM 825 CB ALA A 173 99.668 21.896 8.619 1.00 32.72 A ATOM 826 C ALA A 173 101.005 23.400 7.152 1.00 33.67 A ATOM 827 O ALA A 173 102.125 23.817 7.438 1.00 33.78 A ATOM 828 N ILE A 174 100.698 22.995 5.926 1.00 33.50 A ATOM 829 CA ILE A 174 101.728 23.030 4.896 1.00 33.22 A ATOM 830 CB ILE A 174 101.731 21.736 4.043 1.00 33.98 A ATOM 831 CG2 ILE A 174 101.725 20.502 4.950 1.00 32.94 A ATOM 832 CG1 ILE A 174 100.517 21.709 3.125 1.00 33.93 A ATOM 833 CD1 ILE A 174 100.602 20.631 2.080 1.00 36.79 A ATOM 834 C ILE A 174 101.638 24.231 3.957 1.00 32.69 A ATOM 835 O ILE A 174 102.326 24.269 2.938 1.00 33.88 A ATOM 836 N GLY A 175 100.792 25.204 4.287 1.00 31.76 A ATOM 837 CA GLY A 175 100.671 26.386 3.446 1.00 32.03 A ATOM 838 C GLY A 175 99.838 26.223 2.184 1.00 32.77 A ATOM 839 O GLY A 175 98.870 26.958 1.976 1.00 35.12 A ATOM 840 N SER A 176 100.225 25.291 1.322 1.00 31.63 A ATOM 841 CA SER A 176 99.489 25.018 0.091 1.00 31.11 A ATOM 842 CB SER A 176 99.810 26.040 −0.996 1.00 31.54 A ATOM 843 OG SER A 176 101.141 25.874 −1.464 1.00 33.96 A ATOM 844 C SER A 176 99.946 23.640 −0.354 1.00 30.72 A ATOM 845 O SER A 176 100.977 23.154 0.111 1.00 31.29 A ATOM 846 N PHE A 177 99.180 23.018 −1.246 1.00 28.27 A ATOM 847 CA PHE A 177 99.475 21.683 −1.738 1.00 26.97 A ATOM 848 CB PHE A 177 98.169 20.948 −2.060 1.00 27.18 A ATOM 849 CG PHE A 177 97.376 20.530 −0.854 1.00 27.90 A ATOM 850 CD1 PHE A 177 97.551 21.155 0.379 1.00 26.91 A ATOM 851 CD2 PHE A 177 96.432 19.503 −0.957 1.00 27.62 A ATOM 852 CE1 PHE A 177 96.812 20.762 1.477 1.00 26.03 A ATOM 853 CE2 PHE A 177 95.684 19.106 0.144 1.00 23.95 A ATOM 854 CZ PHE A 177 95.873 19.730 1.357 1.00 25.81 A ATOM 855 C PHE A 177 100.299 21.726 −3.008 1.00 26.99 A ATOM 856 O PHE A 177 100.115 22.618 −3.832 1.00 27.45 A ATOM 857 N ASP A 178 101.200 20.762 −3.179 1.00 26.09 A ATOM 858 CA ASP A 178 101.967 20.704 −4.411 1.00 26.09 A ATOM 859 CB ASP A 178 103.135 19.730 −4.303 1.00 27.73 A ATOM 860 CG ASP A 178 102.689 18.318 −4.023 1.00 33.79 A ATOM 861 OD1 ASP A 178 101.601 17.919 −4.510 1.00 37.57 A ATOM 862 OD2 ASP A 178 103.431 17.590 −3.324 1.00 35.89 A ATOM 863 C ASP A 178 100.955 20.202 −5.443 1.00 25.72 A ATOM 864 O ASP A 178 99.763 20.063 −5.128 1.00 24.80 A ATOM 865 N GLU A 179 101.419 19.897 −6.650 1.00 24.80 A ATOM 866 CA GLU A 179 100.514 19.444 −7.697 1.00 25.67 A ATOM 867 CB GLU A 179 101.187 19.554 −9.052 1.00 27.44 A ATOM 868 CG GLU A 179 100.197 19.921 −10.129 1.00 31.17 A ATOM 869 CD GLU A 179 100.823 19.999 −11.492 1.00 35.24 A ATOM 870 OE1 GLU A 179 102.016 20.372 −11.572 1.00 35.82 A ATOM 871 OE2 GLU A 179 100.116 19.707 −12.488 1.00 38.12 A ATOM 872 C GLU A 179 99.917 18.041 −7.560 1.00 24.90 A ATOM 873 O GLU A 179 98.755 17.822 −7.894 1.00 23.01 A ATOM 874 N THR A 180 100.709 17.095 −7.082 1.00 24.57 A ATOM 875 CA THR A 180 100.240 15.723 −6.923 1.00 25.53 A ATOM 876 CB THR A 180 101.395 14.803 −6.478 1.00 24.65 A ATOM 877 OG1 THR A 180 102.525 15.069 −7.304 1.00 25.84 A ATOM 878 CG2 THR A 180 101.021 13.334 −6.624 1.00 23.39 A ATOM 879 C THR A 180 99.110 15.623 −5.902 1.00 25.85 A ATOM 880 O THR A 180 98.149 14.892 −6.111 1.00 25.59 A ATOM 881 N CYS A 181 99.237 16.359 −4.799 1.00 25.83 A ATOM 882 CA CYS A 181 98.217 16.355 −3.752 1.00 26.26 A ATOM 883 CB CYS A 181 98.778 16.939 −2.451 1.00 27.81 A ATOM 884 SG CYS A 181 100.202 16.031 −1.775 1.00 32.72 A ATOM 885 C CYS A 181 96.963 17.127 −4.169 1.00 25.20 A ATOM 886 O CYS A 181 95.853 16.696 −3.878 1.00 26.19 A ATOM 887 N THR A 182 97.139 18.262 −4.841 1.00 22.74 A ATOM 888 CA THR A 182 96.002 19.046 −5.305 1.00 21.82 A ATOM 889 CB THR A 182 96.453 20.308 −6.103 1.00 21.81 A ATOM 890 OG1 THR A 182 97.258 21.161 −5.276 1.00 24.55 A ATOM 891 CG2 THR A 182 95.252 21.080 −6.593 1.00 18.62 A ATOM 892 C THR A 182 95.197 18.141 −6.249 1.00 23.45 A ATOM 893 O THR A 182 93.975 17.997 −6.116 1.00 22.94 A ATOM 894 N ARG A 183 95.897 17.528 −7.202 1.00 22.71 A ATOM 895 CA ARG A 183 95.260 16.648 −8.158 1.00 23.26 A ATOM 896 CB ARG A 183 96.285 16.118 −9.171 1.00 22.46 A ATOM 897 CG ARG A 183 95.692 15.140 −10.184 1.00 24.96 A ATOM 898 CD ARG A 183 96.762 14.512 −11.078 1.00 27.09 A ATOM 899 NE ARG A 183 97.372 15.577 −11.849 1.00 33.02 A ATOM 900 CZ ARG A 183 98.637 15.948 −11.732 1.00 33.62 A ATOM 901 NH1 ARG A 183 99.440 15.312 −10.885 1.00 32.57 A ATOM 902 NH2 ARG A 183 99.069 17.006 −12.404 1.00 33.25 A ATOM 903 C ARG A 183 94.559 15.475 −7.459 1.00 22.42 A ATOM 904 O ARG A 183 93.393 15.193 −7.721 1.00 21.37 A ATOM 905 N PHE A 184 95.255 14.800 −6.562 1.00 21.19 A ATOM 906 CA PHE A 184 94.630 13.673 −5.888 1.00 22.20 A ATOM 907 CB PHE A 184 95.615 12.964 −4.966 1.00 23.58 A ATOM 908 CG PHE A 184 95.029 11.766 −4.283 1.00 25.43 A ATOM 909 CD1 PHE A 184 94.916 10.556 −4.954 1.00 25.01 A ATOM 910 CD2 PHE A 184 94.508 11.867 −2.998 1.00 24.35 A ATOM 911 CE1 PHE A 184 94.285 9.460 −4.356 1.00 23.50 A ATOM 912 CE2 PHE A 184 93.881 10.782 −2.409 1.00 24.71 A ATOM 913 CZ PHE A 184 93.771 9.577 −3.094 1.00 22.95 A ATOM 914 C PHE A 184 93.405 14.074 −5.072 1.00 21.96 A ATOM 915 O PHE A 184 92.348 13.450 −5.170 1.00 21.31 A ATOM 916 N TYR A 185 93.544 15.116 −4.267 1.00 21.18 A ATOM 917 CA TYR A 185 92.433 15.543 −3.445 1.00 20.50 A ATOM 918 CB TYR A 185 92.956 16.425 −2.313 1.00 21.33 A ATOM 919 CG TYR A 185 93.494 15.550 −1.190 1.00 22.24 A ATOM 920 CD1 TYR A 185 92.641 14.670 −0.507 1.00 21.55 A ATOM 921 CE1 TYR A 185 93.127 13.755 0.414 1.00 20.71 A ATOM 922 CD2 TYR A 185 94.853 15.497 −0.904 1.00 21.37 A ATOM 923 CE2 TYR A 185 95.353 14.579 0.019 1.00 21.80 A ATOM 924 CZ TYR A 185 94.486 13.705 0.670 1.00 21.18 A ATOM 925 OH TYR A 185 94.986 12.746 1.519 1.00 19.84 A ATOM 926 C TYR A 185 91.273 16.182 −4.201 1.00 19.27 A ATOM 927 O TYR A 185 90.112 16.056 −3.801 1.00 17.72 A ATOM 928 N THR A 186 91.576 16.834 −5.314 1.00 17.25 A ATOM 929 CA THR A 186 90.527 17.433 −6.110 1.00 15.61 A ATOM 930 CB THR A 186 91.097 18.366 −7.188 1.00 15.69 A ATOM 931 OG1 THR A 186 91.710 19.508 −6.564 1.00 16.11 A ATOM 932 CG2 THR A 186 89.996 18.816 −8.135 1.00 12.68 A ATOM 933 C THR A 186 89.756 16.302 −6.785 1.00 15.75 A ATOM 934 O THR A 186 88.523 16.350 −6.899 1.00 16.51 A ATOM 935 N ALA A 187 90.478 15.277 −7.218 1.00 14.94 A ATOM 936 CA ALA A 187 89.841 14.136 −7.868 1.00 16.15 A ATOM 937 CB ALA A 187 90.905 13.130 −8.382 1.00 13.30 A ATOM 938 C ALA A 187 88.847 13.450 −6.911 1.00 16.71 A ATOM 939 O ALA A 187 87.743 13.075 −7.328 1.00 16.50 A ATOM 940 N GLU A 188 89.213 13.308 −5.635 1.00 17.10 A ATOM 941 CA GLU A 188 88.302 12.673 −4.679 1.00 17.85 A ATOM 942 CB GLU A 188 88.953 12.514 −3.302 1.00 18.83 A ATOM 943 CG GLU A 188 90.219 11.665 −3.296 1.00 19.46 A ATOM 944 CD GLU A 188 90.370 10.795 −2.050 1.00 20.84 A ATOM 945 OE1 GLU A 188 90.131 11.276 −0.920 1.00 21.14 A ATOM 946 OE2 GLU A 188 90.749 9.616 −2.207 1.00 23.35 A ATOM 947 C GLU A 188 87.043 13.516 −4.551 1.00 17.79 A ATOM 948 O GLU A 188 85.921 13.005 −4.579 1.00 18.83 A ATOM 949 N ILE A 189 87.220 14.824 −4.449 1.00 17.09 A ATOM 950 CA ILE A 189 86.060 15.688 −4.312 1.00 15.61 A ATOM 951 CB ILE A 189 86.495 17.141 −4.054 1.00 15.83 A ATOM 952 CG2 ILE A 189 85.278 18.019 −3.853 1.00 14.16 A ATOM 953 CG1 ILE A 189 87.380 17.199 −2.794 1.00 17.34 A ATOM 954 CD1 ILE A 189 87.949 18.583 −2.479 1.00 15.37 A ATOM 955 C ILE A 189 85.176 15.611 −5.558 1.00 16.00 A ATOM 956 O ILE A 189 83.953 15.530 −5.460 1.00 15.52 A ATOM 957 N VAL A 190 85.794 15.619 −6.733 1.00 15.46 A ATOM 958 CA VAL A 190 85.031 15.570 −7.964 1.00 15.38 A ATOM 959 CB VAL A 190 85.975 15.641 −9.181 1.00 15.37 A ATOM 960 CG1 VAL A 190 85.273 15.168 −10.447 1.00 14.43 A ATOM 961 CG2 VAL A 190 86.454 17.056 −9.350 1.00 14.03 A ATOM 962 C VAL A 190 84.228 14.279 −7.987 1.00 17.35 A ATOM 963 O VAL A 190 83.016 14.281 −8.258 1.00 15.96 A ATOM 964 N SER A 191 84.916 13.182 −7.683 1.00 17.90 A ATOM 965 CA SER A 191 84.305 11.858 −7.660 1.00 17.77 A ATOM 966 CB SER A 191 85.377 10.811 −7.344 1.00 18.25 A ATOM 967 OG SER A 191 84.801 9.523 −7.243 1.00 21.13 A ATOM 968 C SER A 191 83.147 11.778 −6.640 1.00 17.28 A ATOM 969 O SER A 191 82.153 11.095 −6.865 1.00 15.44 A ATOM 970 N ALA A 192 83.291 12.490 −5.525 1.00 17.27 A ATOM 971 CA ALA A 192 82.267 12.529 −4.485 1.00 15.98 A ATOM 972 CB ALA A 192 82.834 13.164 −3.191 1.00 14.89 A ATOM 973 C ALA A 192 81.078 13.336 −4.988 1.00 16.44 A ATOM 974 O ALA A 192 79.934 12.922 −4.816 1.00 17.59 A ATOM 975 N LEU A 193 81.340 14.487 −5.609 1.00 16.63 A ATOM 976 CA LEU A 193 80.253 15.303 −6.140 1.00 16.11 A ATOM 977 CB LEU A 193 80.769 16.632 −6.688 1.00 16.40 A ATOM 978 CG LEU A 193 81.421 17.545 −5.645 1.00 18.83 A ATOM 979 CD1 LEU A 193 81.779 18.885 −6.276 1.00 18.24 A ATOM 980 CD2 LEU A 193 80.455 17.751 −4.479 1.00 18.63 A ATOM 981 C LEU A 193 79.509 14.551 −7.236 1.00 16.95 A ATOM 982 O LEU A 193 78.286 14.623 −7.325 1.00 18.76 A ATOM 983 N GLU A 194 80.229 13.825 −8.079 1.00 17.87 A ATOM 984 CA GLU A 194 79.539 13.082 −9.124 1.00 19.66 A ATOM 985 CB GLU A 194 80.525 12.295 −9.990 1.00 21.82 A ATOM 986 CG GLU A 194 79.844 11.333 −10.947 1.00 21.12 A ATOM 987 CD GLU A 194 80.831 10.513 −11.758 1.00 25.70 A ATOM 988 OE1 GLU A 194 81.900 10.122 −11.216 1.00 27.41 A ATOM 989 OE2 GLU A 194 80.527 10.244 −12.939 1.00 26.12 A ATOM 990 C GLU A 194 78.546 12.123 −8.479 1.00 19.58 A ATOM 991 O GLU A 194 77.420 11.987 −8.937 1.00 17.78 A ATOM 992 N TYR A 195 78.962 11.462 −7.406 1.00 19.09 A ATOM 993 CA TYR A 195 78.063 10.545 −6.736 1.00 19.86 A ATOM 994 CB TYR A 195 78.807 9.740 −5.673 1.00 20.01 A ATOM 995 CG TYR A 195 77.871 8.975 −4.756 1.00 20.45 A ATOM 996 CD1 TYR A 195 77.329 7.748 −5.142 1.00 19.40 A ATOM 997 CE1 TYR A 195 76.471 7.044 −4.296 1.00 18.43 A ATOM 998 CD2 TYR A 195 77.527 9.48 −3.500 1.00 20.11 A ATOM 999 CE2 TYR A 195 76.678 8.79 −2.652 1.00 19.96 A ATOM 1000 CZ TYR A 195 76.154 7.567 −3.057 1.00 21.07 A ATOM 1001 OH TYR A 195 75.336 6.859 −2.206 1.00 21.31 A ATOM 1002 C TYR A 195 76.914 11.295 −6.060 1.00 20.00 A ATOM 1003 O TYR A 195 75.775 10.823 −6.033 1.00 21.42 A ATOM 1004 N LEU A 196 77.222 12.455 −5.500 1.00 17.38 A ATOM 1005 CA LEU A 196 76.209 13.226 −4.795 1.00 18.74 A ATOM 1006 CB LEU A 196 76.846 14.412 −4.049 1.00 17.38 A ATOM 1007 CG LEU A 196 75.850 15.100 −3.110 1.00 19.04 A ATOM 1008 CD1 LEU A 196 75.423 14.093 −2.061 1.00 17.66 A ATOM 1009 CD2 LEU A 196 76.462 16.338 −2.453 1.00 19.54 A ATOM 1010 C LEU A 196 75.148 13.747 −5.751 1.00 18.47 A ATOM 1011 O LEU A 196 73.944 13.608 −5.523 1.00 15.05 A ATOM 1012 N HIS A 197 75.622 14.361 −6.824 1.00 18.35 A ATOM 1013 CA HIS A 197 74.740 14.915 −7.812 1.00 20.04 A ATOM 1014 CB HIS A 197 75.562 15.809 −8.718 1.00 20.29 A ATOM 1015 CG HIS A 197 76.048 17.044 −8.025 1.00 21.90 A ATOM 1016 CD2 HIS A 197 75.766 17.539 −6.794 1.00 19.49 A ATOM 1017 ND1 HIS A 197 76.892 17.956 −8.621 1.00 20.69 A ATOM 1018 CE1 HIS A 197 77.104 18.960 −7.789 1.00 20.86 A ATOM 1019 NE2 HIS A 197 76.433 18.732 −6.676 1.00 19.12 A ATOM 1020 C HIS A 197 73.950 13.858 −8.587 1.00 21.27 A ATOM 1021 O HIS A 197 72.865 14.133 −9.099 1.00 21.23 A ATOM 1022 N GLY A 198 74.487 12.644 −8.644 1.00 21.36 A ATOM 1023 CA GLY A 198 73.810 11.569 −9.339 1.00 20.60 A ATOM 1024 C GLY A 198 72.528 11.203 −8.632 1.00 22.72 A ATOM 1025 O GLY A 198 71.593 10.742 −9.269 1.00 22.75 A ATOM 1026 N LYS A 199 72.478 11.411 −7.313 1.00 24.27 A ATOM 1027 CA LYS A 199 71.280 11.105 −6.523 1.00 22.95 A ATOM 1028 CB LYS A 199 71.659 10.629 −5.123 1.00 24.67 A ATOM 1029 CG LYS A 199 72.570 9.429 −5.109 1.00 29.22 A ATOM 1030 CD LYS A 199 72.986 9.064 −3.701 1.00 33.11 A ATOM 1031 CE LYS A 199 72.531 7.660 −3.366 1.00 37.28 A ATOM 1032 NZ LYS A 199 72.917 6.686 −4.455 1.00 38.82 A ATOM 1033 C LYS A 199 70.432 12.354 −6.398 1.00 22.39 A ATOM 1034 O LYS A 199 69.558 12.431 −5.542 1.00 22.53 A ATOM 1035 N GLY A 200 70.710 13.343 −7.241 1.00 21.56 A ATOM 1036 CA GLY A 200 69.953 14.580 −7.203 1.00 22.28 A ATOM 1037 C GLY A 200 70.006 15.326 −5.882 1.00 23.53 A ATOM 1038 O GLY A 200 69.017 15.930 −5.461 1.00 24.83 A ATOM 1039 N ILE A 201 71.161 15.302 −5.225 1.00 22.74 A ATOM 1040 CA ILE A 201 71.314 15.985 −3.951 1.00 22.95 A ATOM 1041 CB ILE A 201 71.796 15.007 −2.842 1.00 22.51 A ATOM 1042 CG2 ILE A 201 71.995 15.757 −1.536 1.00 21.73 A ATOM 1043 CG1 ILE A 201 70.788 13.876 −2.638 1.00 22.48 A ATOM 1044 CD1 ILE A 201 71.274 12.791 −1.687 1.00 17.26 A ATOM 1045 C ILE A 201 72.361 17.086 −4.076 1.00 24.41 A ATOM 1046 O ILE A 201 73.387 16.904 −4.737 1.00 26.41 A ATOM 1047 N ILE A 202 72.118 18.236 −3.470 1.00 23.00 A ATOM 1048 CA ILE A 202 73.137 19.267 −3.520 1.00 24.60 A ATOM 1049 CB ILE A 202 72.729 20.440 −4.420 1.00 26.37 A ATOM 1050 CG2 ILE A 202 72.503 19.934 −5.829 1.00 28.52 A ATOM 1051 CG1 ILE A 202 71.450 21.086 −3.922 1.00 29.04 A ATOM 1052 CD1 ILE A 202 70.958 22.165 −4.845 1.00 32.55 A ATOM 1053 C ILE A 202 73.482 19.732 −2.105 1.00 24.36 A ATOM 1054 O ILE A 202 72.605 19.919 −1.257 1.00 25.89 A ATOM 1055 N HIS A 203 74.776 19.882 −1.856 1.00 22.94 A ATOM 1056 CA HIS A 203 75.289 20.273 −0.555 1.00 22.27 A ATOM 1057 CB HIS A 203 76.800 20.010 −0.526 1.00 20.00 A ATOM 1058 CG HIS A 203 77.401 20.051 0.840 1.00 18.45 A ATOM 1059 CD2 HIS A 203 77.865 19.060 1.640 1.00 19.77 A ATOM 1060 ND1 HIS A 203 77.569 21.222 1.542 1.00 16.33 A ATOM 1061 CE1 HIS A 203 78.115 20.953 2.715 1.00 17.77 A ATOM 1062 NE2 HIS A 203 78.306 19.650 2.800 1.00 18.48 A ATOM 1063 C HIS A 203 74.978 21.731 −0.206 1.00 23.37 A ATOM 1064 O HIS A 203 74.411 22.009 0.860 1.00 22.52 A ATOM 1065 N ARG A 204 75.361 22.648 −1.101 1.00 23.22 A ATOM 1066 CA ARG A 204 75.126 24.087 −0.934 1.00 23.42 A ATOM 1067 CB ARG A 204 73.674 24.375 −0.544 1.00 22.74 A ATOM 1068 CG ARG A 204 72.663 23.966 −1.561 1.00 24.57 A ATOM 1069 CD ARG A 204 71.341 24.681 −1.325 1.00 26.51 A ATOM 1070 NE ARG A 204 70.699 24.299 −0.074 1.00 28.25 A ATOM 1071 CZ ARG A 204 69.596 24.871 0.405 1.00 28.63 A ATOM 1072 NH1 ARG A 204 69.013 25.849 −0.267 1.00 28.47 A ATOM 1073 NH2 ARG A 204 69.086 24.472 1.563 1.00 28.55 A ATOM 1074 C ARG A 204 76.017 24.819 0.061 1.00 24.12 A ATOM 1075 O ARG A 204 75.805 26.001 0.308 1.00 26.26 A ATOM 1076 N ASP A 205 76.990 24.135 0.654 1.00 23.05 A ATOM 1077 CA ASP A 205 77.887 24.789 1.595 1.00 20.96 A ATOM 1078 CB ASP A 205 77.219 24.883 2.964 1.00 22.31 A ATOM 1079 CG ASP A 205 77.964 25.801 3.914 1.00 26.08 A ATOM 1080 OD1 ASP A 205 78.812 26.582 3.439 1.00 25.93 A ATOM 1081 OD2 ASP A 205 77.707 25.751 5.141 1.00 29.89 A ATOM 1082 C ASP A 205 79.210 24.020 1.662 1.00 20.46 A ATOM 1083 O ASP A 205 79.812 23.833 2.716 1.00 21.36 A ATOM 1084 N LEU A 206 79.666 23.584 0.504 1.00 18.98 A ATOM 1085 CA LEU A 206 80.893 22.827 0.407 1.00 19.83 A ATOM 1086 CB LEU A 206 80.983 22.229 −0.994 1.00 21.73 A ATOM 1087 CG LEU A 206 82.039 21.167 −1.298 1.00 24.76 A ATOM 1088 CD1 LEU A 206 81.818 19.943 −0.401 1.00 24.95 A ATOM 1089 CD2 LEU A 206 81.941 20.789 −2.778 1.00 23.74 A ATOM 1090 C LEU A 206 82.093 23.725 0.691 1.00 20.17 A ATOM 1091 O LEU A 206 82.162 24.857 0.200 1.00 20.92 A ATOM 1092 N LYS A 207 83.044 23.226 1.475 1.00 19.79 A ATOM 1093 CA LYS A 207 84.233 24.004 1.821 1.00 19.45 A ATOM 1094 CB LYS A 207 83.825 25.209 2.667 1.00 17.84 A ATOM 1095 CG LYS A 207 83.123 24.820 3.933 1.00 19.19 A ATOM 1096 CD LYS A 207 82.331 25.969 4.500 1.00 20.50 A ATOM 1097 CE LYS A 207 81.663 25.556 5.797 1.00 22.10 A ATOM 1098 NZ LYS A 207 80.955 26.674 6.480 1.00 22.34 A ATOM 1099 C LYS A 207 85.241 23.130 2.565 1.00 19.59 A ATOM 1100 O LYS A 207 84.917 22.025 2.985 1.00 20.21 A ATOM 1101 N PRO A 208 86.480 23.618 2.737 1.00 19.79 A ATOM 1102 CD PRO A 208 87.032 24.869 2.188 1.00 18.04 A ATOM 1103 CA PRO A 208 87.526 22.853 3.428 1.00 19.22 A ATOM 1104 CB PRO A 208 88.756 23.763 3.297 1.00 19.27 A ATOM 1105 CG PRO A 208 88.496 24.521 2.027 1.00 16.27 A ATOM 1106 C PRO A 208 87.221 22.477 4.883 1.00 20.50 A ATOM 1107 O PRO A 208 87.791 21.511 5.411 1.00 21.44 A ATOM 1108 N GLU A 209 86.335 23.231 5.530 1.00 20.19 A ATOM 1109 CA GLU A 209 85.956 22.976 6.927 1.00 21.25 A ATOM 1110 CB GLU A 209 85.383 24.251 7.562 1.00 21.43 A ATOM 1111 CG GLU A 209 86.330 25.446 7.535 1.00 26.33 A ATOM 1112 CD GLU A 209 86.203 26.315 6.270 1.00 30.17 A ATOM 1113 OE1 GLU A 209 86.143 25.785 5.131 1.00 30.44 A ATOM 1114 OE2 GLU A 209 86.173 27.557 6.422 1.00 33.49 A ATOM 1115 C GLU A 209 84.920 21.839 7.040 1.00 22.45 A ATOM 1116 O GLU A 209 84.733 21.255 8.114 1.00 21.98 A ATOM 1117 N ASN A 210 84.269 21.545 5.915 1.00 22.73 A ATOM 1118 CA ASN A 210 83.234 20.514 5.788 1.00 23.66 A ATOM 1119 CB ASN A 210 82.102 21.013 4.882 1.00 26.67 A ATOM 1120 CG ASN A 210 81.104 21.881 5.613 1.00 33.39 A ATOM 1121 OD1 ASN A 210 80.223 22.481 4.988 1.00 36.52 A ATOM 1122 ND2 ASN A 210 81.221 21.950 6.946 1.00 34.23 A ATOM 1123 C ASN A 210 83.775 19.239 5.162 1.00 21.41 A ATOM 1124 O ASN A 210 83.067 18.244 5.081 1.00 21.16 A ATOM 1125 N ILE A 211 85.006 19.293 4.674 1.00 19.42 A ATOM 1126 CA ILE A 211 85.619 18.141 4.029 1.00 17.43 A ATOM 1127 CB ILE A 211 86.319 18.556 2.708 1.00 14.89 A ATOM 1128 CG2 ILE A 211 87.046 17.349 2.096 1.00 12.68 A ATOM 1129 CG1 ILE A 211 85.277 19.157 1.736 1.00 13.30 A ATOM 1130 CD1 ILE A 211 85.855 19.805 0.435 1.00 10.47 A ATOM 1131 C ILE A 211 86.620 17.578 5.024 1.00 17.83 A ATOM 1132 O ILE A 211 87.685 18.151 5.241 1.00 17.76 A ATOM 1133 N LEU A 212 86.265 16.457 5.639 1.00 16.05 A ATOM 1134 CA LEU A 212 87.121 15.871 6.656 1.00 15.84 A ATOM 1135 CB LEU A 212 86.256 15.319 7.793 1.00 14.28 A ATOM 1136 CG LEU A 212 85.108 16.227 8.285 1.00 14.68 A ATOM 1137 CD1 LEU A 212 84.606 15.715 9.647 1.00 11.38 A ATOM 1138 CD2 LEU A 212 85.579 17.685 8.422 1.00 10.88 A ATOM 1139 C LEU A 212 88.031 14.787 6.114 1.00 16.77 A ATOM 1140 O LEU A 212 87.861 14.335 4.984 1.00 16.78 A ATOM 1141 N LEU A 213 88.999 14.374 6.925 1.00 16.47 A ATOM 1142 CA LEU A 213 89.924 13.332 6.516 1.00 17.64 A ATOM 1143 CB LEU A 213 91.323 13.926 6.378 1.00 18.08 A ATOM 1144 CG LEU A 213 91.367 14.880 5.176 1.00 17.92 A ATOM 1145 CD1 LEU A 213 92.076 16.134 5.529 1.00 18.78 A ATOM 1146 CD2 LEU A 213 92.042 14.187 4.000 1.00 17.07 A ATOM 1147 C LEU A 213 89.919 12.147 7.473 1.00 18.68 A ATOM 1148 O LEU A 213 90.091 12.297 8.672 1.00 18.75 A ATOM 1149 N ASN A 214 89.712 10.955 6.939 1.00 21.19 A ATOM 1150 CA ASN A 214 89.673 9.780 7.797 1.00 23.68 A ATOM 1151 CB ASN A 214 88.864 8.657 7.122 1.00 25.68 A ATOM 1152 CG ASN A 214 89.613 7.979 6.012 1.00 31.70 A ATOM 1153 OD1 ASN A 214 90.680 8.426 5.590 1.00 35.54 A ATOM 1154 ND2 ASN A 214 89.057 6.886 5.521 1.00 34.56 A ATOM 1155 C ASN A 214 91.077 9.328 8.203 1.00 22.08 A ATOM 1156 O ASN A 214 92.056 9.972 7.864 1.00 20.25 A ATOM 1157 N ALA A 215 91.170 8.239 8.953 1.00 24.03 A ATOM 1158 CA ALA A 215 92.464 7.738 9.420 1.00 24.26 A ATOM 1159 CB ALA A 215 92.276 6.502 10.277 1.00 21.70 A ATOM 1160 C ALA A 215 93.421 7.426 8.296 1.00 24.90 A ATOM 1161 O ALA A 215 94.615 7.435 8.491 1.00 26.03 A ATOM 1162 N ASP A 216 92.889 7.143 7.108 1.00 25.93 A ATOM 1163 CA ASP A 216 93.726 6.826 5.963 1.00 26.29 A ATOM 1164 CB ASP A 216 93.048 5.773 5.091 1.00 32.31 A ATOM 1165 CG ASP A 216 92.862 4.456 5.812 1.00 38.06 A ATOM 1166 OD1 ASP A 216 93.780 4.043 6.559 1.00 40.03 A ATOM 1167 OD2 ASP A 216 91.800 3.823 5.616 1.00 42.79 A ATOM 1168 C ASP A 216 94.046 8.026 5.095 1.00 23.69 A ATOM 1169 O ASP A 216 94.717 7.899 4.085 1.00 24.38 A ATOM 1170 N MET A 217 93.546 9.187 5.478 1.00 21.45 A ATOM 1171 CA MET A 217 93.752 10.418 4.726 1.00 20.48 A ATOM 1172 CB MET A 217 95.226 10.614 4.396 1.00 21.48 A ATOM 1173 CG MET A 217 96.081 10.894 5.629 1.00 21.46 A ATOM 1174 SD MET A 217 95.504 12.311 6.580 1.00 25.32 A ATOM 1175 CE MET A 217 96.079 13.722 5.573 1.00 24.08 A ATOM 1176 C MET A 217 92.900 10.556 3.458 1.00 19.63 A ATOM 1177 O MET A 217 93.245 11.294 2.546 1.00 19.54 A ATOM 1178 N HIS A 218 91.794 9.824 3.405 1.00 18.82 A ATOM 1179 CA HIS A 218 90.843 9.945 2.311 1.00 18.81 A ATOM 1180 CB HIS A 218 90.206 8.589 1.994 1.00 20.61 A ATOM 1181 CG HIS A 218 91.097 7.666 1.218 1.00 22.68 A ATOM 1182 CD2 HIS A 218 91.840 6.605 1.614 1.00 20.37 A ATOM 1183 ND1 HIS A 218 91.316 7.806 −0.139 1.00 21.30 A ATOM 1184 CE1 HIS A 218 92.153 6.867 −0.541 1.00 20.75 A ATOM 1185 NE2 HIS A 218 92.485 6.128 0.501 1.00 20.31 A ATOM 1186 C HIS A 218 89.774 10.925 2.863 1.00 18.97 A ATOM 1187 O HIS A 218 89.534 10.965 4.083 1.00 16.48 A ATOM 1188 N ILE A 219 89.166 11.721 1.978 1.00 17.41 A ATOM 1189 CA ILE A 219 88.165 12.702 2.387 1.00 16.48 A ATOM 1190 CB ILE A 219 87.765 13.695 1.242 1.00 13.43 A ATOM 1191 CG2 ILE A 219 88.984 14.404 0.698 1.00 10.66 A ATOM 1192 CG1 ILE A 219 86.973 12.952 0.156 1.00 11.14 A ATOM 1193 CD1 ILE A 219 86.505 13.807 −0.995 1.00  4.26 A ATOM 1194 C ILE A 219 86.875 12.067 2.864 1.00 17.14 A ATOM 1195 O ILE A 219 86.541 10.943 2.497 1.00 18.77 A ATOM 1196 N GLN A 220 86.159 12.808 3.696 1.00 17.24 A ATOM 1197 CA GLN A 220 84.878 12.376 4.203 1.00 18.93 A ATOM 1198 CB GLN A 220 85.002 11.756 5.604 1.00 22.02 A ATOM 1199 CG GLN A 220 83.791 10.874 5.952 1.00 26.68 A ATOM 1200 CD GLN A 220 83.949 10.071 7.253 1.00 31.76 A ATOM 1201 OE1 GLN A 220 83.437 10.471 8.331 1.00 27.57 A ATOM 1202 NE2 GLN A 220 84.667 8.930 7.161 1.00 29.97 A ATOM 1203 C GLN A 220 84.077 13.652 4.261 1.00 17.44 A ATOM 1204 O GLN A 220 84.247 14.465 5.170 1.00 17.81 A ATOM 1205 N ILE A 221 83.229 13.852 3.263 1.00 15.69 A ATOM 1206 CA ILE A 221 82.413 15.051 3.230 1.00 16.08 A ATOM 1207 CB ILE A 221 81.939 15.359 1.802 1.00 15.82 A ATOM 1208 CG2 ILE A 221 80.956 16.519 1.834 1.00 13.95 A ATOM 1209 CG1 ILE A 221 83.163 15.627 0.899 1.00 16.66 A ATOM 1210 CD1 ILE A 221 82.837 16.045 −0.548 1.00 13.13 A ATOM 1211 C ILE A 221 81.207 14.892 4.156 1.00 16.52 A ATOM 1212 O ILE A 221 80.542 13.860 4.157 1.00 16.03 A ATOM 1213 N THR A 222 80.927 15.922 4.948 1.00 17.66 A ATOM 1214 CA THR A 222 79.810 15.862 5.882 1.00 17.70 A ATOM 1215 CB THR A 222 80.331 15.433 7.277 1.00 18.71 A ATOM 1216 OG1 THR A 222 79.230 15.263 8.172 1.00 16.76 A ATOM 1217 CG2 THR A 222 81.319 16.470 7.825 1.00 16.79 A ATOM 1218 C THR A 222 79.069 17.195 5.980 1.00 17.35 A ATOM 1219 O THR A 222 79.246 18.062 5.130 1.00 16.83 A ATOM 1220 N ASP A 223 78.244 17.344 7.018 1.00 18.09 A ATOM 1221 CA ASP A 223 77.466 18.567 7.268 1.00 19.60 A ATOM 1222 CB ASP A 223 78.403 19.778 7.311 1.00 22.73 A ATOM 1223 CG ASP A 223 77.763 21.006 7.959 1.00 28.30 A ATOM 1224 OD1 ASP A 223 76.565 20.931 8.335 1.00 28.17 A ATOM 1225 OD2 ASP A 223 78.480 22.042 8.081 1.00 30.99 A ATOM 1226 C ASP A 223 76.382 18.799 6.210 1.00 19.52 A ATOM 1227 O ASP A 223 76.528 19.655 5.340 1.00 19.39 A ATOM 1228 N PHE A 224 75.283 18.058 6.303 1.00 18.74 A ATOM 1229 CA PHE A 224 74.213 18.168 5.321 1.00 18.81 A ATOM 1230 CB PHE A 224 73.825 16.773 4.853 1.00 17.07 A ATOM 1231 CG PHE A 224 74.857 16.150 3.971 1.00 17.01 A ATOM 1232 CD1 PHE A 224 74.751 16.250 2.578 1.00 16.10 A ATOM 1233 CD2 PHE A 224 75.982 15.543 4.521 1.00 14.00 A ATOM 1234 CE1 PHE A 224 75.761 15.752 1.747 1.00 15.92 A ATOM 1235 CE2 PHE A 224 77.001 15.042 3.699 1.00 15.63 A ATOM 1236 CZ PHE A 224 76.889 15.147 2.309 1.00 15.79 A ATOM 1237 C PHE A 224 72.997 18.932 5.775 1.00 19.88 A ATOM 1238 O PHE A 224 71.961 18.922 5.115 1.00 19.36 A ATOM 1239 N GLY A 225 73.135 19.599 6.911 1.00 21.38 A ATOM 1240 CA GLY A 225 72.046 20.388 7.439 1.00 21.39 A ATOM 1241 C GLY A 225 71.672 21.545 6.523 1.00 23.43 A ATOM 1242 O GLY A 225 70.802 22.323 6.869 1.00 26.22 A ATOM 1243 N THR A 226 72.311 21.692 5.370 1.00 22.15 A ATOM 1244 CA THR A 226 71.930 22.784 4.492 1.00 23.85 A ATOM 1245 CB THR A 226 72.986 23.946 4.465 1.00 24.65 A ATOM 1246 OG1 THR A 226 74.197 23.511 3.830 1.00 24.83 A ATOM 1247 CG2 THR A 226 73.285 24.420 5.866 1.00 23.67 A ATOM 1248 C THR A 226 71.721 22.289 3.073 1.00 24.12 A ATOM 1249 O THR A 226 71.646 23.079 2.129 1.00 22.82 A ATOM 1250 N ALA A 227 71.620 20.976 2.935 1.00 23.84 A ATOM 1251 CA ALA A 227 71.437 20.357 1.637 1.00 26.21 A ATOM 1252 CB ALA A 227 71.774 18.889 1.734 1.00 24.04 A ATOM 1253 C ALA A 227 70.026 20.535 1.064 1.00 28.20 A ATOM 1254 O ALA A 227 69.069 20.767 1.801 1.00 29.29 A ATOM 1255 N ALA A 228 69.912 20.449 −0.258 1.00 28.91 A ATOM 1256 CA ALA A 228 68.623 20.554 −0.928 1.00 31.02 A ATOM 1257 CB ALA A 228 68.577 21.795 −1.856 1.00 30.45 A ATOM 1258 C ALA A 228 68.501 19.276 −1.745 1.00 32.01 A ATOM 1259 O ALA A 228 69.474 18.846 −2.363 1.00 32.87 A ATOM 1260 N VAL A 229 67.328 18.650 −1.732 1.00 32.95 A ATOM 1261 CA VAL A 229 67.126 17.424 −2.503 1.00 34.26 A ATOM 1262 CB VAL A 229 66.468 16.347 −1.657 1.00 33.02 A ATOM 1263 CG1 VAL A 229 66.194 15.114 −2.498 1.00 33.80 A ATOM 1264 CG2 VAL A 229 67.356 16.011 −0.496 1.00 31.38 A ATOM 1265 C VAL A 229 66.213 17.757 −3.665 1.00 36.36 A ATOM 1266 O VAL A 229 65.065 18.133 −3.455 1.00 38.02 A ATOM 1267 N LEU A 230 66.715 17.628 −4.889 1.00 37.75 A ATOM 1268 CA LEU A 230 65.917 17.965 −6.066 1.00 39.87 A ATOM 1269 CB LEU A 230 66.741 17.775 −7.335 1.00 41.23 A ATOM 1270 CG LEU A 230 68.039 18.585 −7.359 1.00 44.16 A ATOM 1271 CD1 LEU A 230 68.843 18.208 −8.599 1.00 43.48 A ATOM 1272 CD2 LEU A 230 67.724 20.087 −7.313 1.00 42.99 A ATOM 1273 C LEU A 230 64.646 17.137 −6.162 1.00 40.59 A ATOM 1274 O LEU A 230 64.703 15.954 −6.486 1.00 41.31 A ATOM 1275 N ASN A 240 65.964 27.756 −2.248 1.00 83.97 A ATOM 1276 CA ASN A 240 66.331 29.165 −2.370 1.00 84.48 A ATOM 1277 CB ASN A 240 65.294 29.907 −3.225 1.00 85.56 A ATOM 1278 CG ASN A 240 63.949 30.053 −2.524 1.00 86.59 A ATOM 1279 OD1 ASN A 240 63.850 30.682 −1.465 1.00 87.31 A ATOM 1280 ND2 ASN A 240 62.904 29.473 −3.115 1.00 86.14 A ATOM 1281 C ASN A 240 66.433 29.828 −0.994 1.00 83.85 A ATOM 1282 O ASN A 240 66.898 30.963 −0.862 1.00 84.11 A ATOM 1283 N ALA A 241 65.997 29.096 0.023 1.00 83.19 A ATOM 1284 CA ALA A 241 65.996 29.564 1.405 1.00 81.85 A ATOM 1285 C ALA A 241 67.330 29.365 2.127 1.00 79.97 A ATOM 1286 O ALA A 241 67.349 28.777 3.214 1.00 79.75 A ATOM 1287 CB ALA A 241 64.894 28.825 2.183 1.00 85.17 A ATOM 1288 N PHE A 242 68.433 29.850 1.551 1.00 77.03 A ATOM 1289 CA PHE A 242 69.737 29.680 2.197 1.00 74.85 A ATOM 1290 CB PHE A 242 69.973 28.183 2.438 1.00 73.81 A ATOM 1291 CG PHE A 242 71.311 27.861 3.015 1.00 72.36 A ATOM 1292 CD1 PHE A 242 71.595 28.116 4.353 1.00 72.39 A ATOM 1293 CD2 PHE A 242 72.297 27.312 2.210 1.00 72.03 A ATOM 1294 CE1 PHE A 242 72.855 27.823 4.879 1.00 72.87 A ATOM 1295 CE2 PHE A 242 73.553 27.016 2.714 1.00 72.25 A ATOM 1296 CZ PHE A 242 73.837 27.270 4.054 1.00 72.96 A ATOM 1297 C PHE A 242 70.951 30.283 1.462 1.00 73.13 A ATOM 1298 O PHE A 242 70.958 30.425 0.233 1.00 74.08 A ATOM 1299 N VAL A 243 71.972 30.625 2.250 1.00 69.64 A ATOM 1300 CA VAL A 243 73.233 31.204 1.777 1.00 65.87 A ATOM 1301 CB VAL A 243 73.207 32.765 1.834 1.00 66.73 A ATOM 1302 CG1 VAL A 243 74.498 33.344 1.271 1.00 65.65 A ATOM 1303 CG2 VAL A 243 72.008 33.299 1.084 1.00 66.83 A ATOM 1304 C VAL A 243 74.349 30.708 2.703 1.00 62.21 A ATOM 1305 O VAL A 243 74.471 31.189 3.839 1.00 61.91 A ATOM 1306 N GLY A 244 75.149 29.760 2.204 1.00 57.62 A ATOM 1307 CA GLY A 244 76.247 29.177 2.967 1.00 51.60 A ATOM 1308 C GLY A 244 77.341 30.132 3.387 1.00 46.47 A ATOM 1309 O GLY A 244 77.063 31.261 3.757 1.00 48.62 A ATOM 1310 N THR A 245 78.588 29.686 3.325 1.00 42.06 A ATOM 1311 CA THR A 245 79.709 30.526 3.726 1.00 36.35 A ATOM 1312 CB THR A 245 80.925 29.673 4.096 1.00 35.76 A ATOM 1313 OG1 THR A 245 80.539 28.740 5.105 1.00 31.66 A ATOM 1314 CG2 THR A 245 82.043 30.534 4.651 1.00 33.72 A ATOM 1315 C THR A 245 80.064 31.524 2.637 1.00 34.43 A ATOM 1316 O THR A 245 80.309 31.166 1.485 1.00 33.95 A ATOM 1317 N ALA A 246 80.087 32.787 3.034 1.00 32.72 A ATOM 1318 CA ALA A 246 80.338 33.900 2.142 1.00 30.18 A ATOM 1319 CB ALA A 246 80.684 35.127 2.952 1.00 30.18 A ATOM 1320 C ALA A 246 81.374 33.678 1.062 1.00 29.56 A ATOM 1321 O ALA A 246 81.099 33.895 −0.113 1.00 30.00 A ATOM 1322 N GLN A 247 82.564 33.242 1.445 1.00 28.03 A ATOM 1323 CA GLN A 247 83.623 33.030 0.468 1.00 26.97 A ATOM 1324 CB GLN A 247 84.929 32.706 1.182 1.00 28.32 A ATOM 1325 CG GLN A 247 85.208 33.659 2.319 1.00 33.33 A ATOM 1326 CD GLN A 247 86.600 33.522 2.863 1.00 36.16 A ATOM 1327 OE1 GLN A 247 87.556 34.107 2.335 1.00 36.68 A ATOM 1328 NE2 GLN A 247 86.738 32.731 3.922 1.00 39.27 A ATOM 1329 C GLN A 247 83.355 31.968 −0.583 1.00 25.04 A ATOM 1330 O GLN A 247 83.962 31.997 −1.653 1.00 25.92 A ATOM 1331 N TYR A 248 82.443 31.045 −0.304 1.00 22.51 A ATOM 1332 CA TYR A 248 82.161 29.970 −1.260 1.00 21.98 A ATOM 1333 CB TYR A 248 82.273 28.613 −0.541 1.00 17.74 A ATOM 1334 CG TYR A 248 83.626 28.444 0.117 1.00 14.83 A ATOM 1335 CD1 TYR A 248 84.736 28.063 −0.630 1.00 14.53 A ATOM 1336 CE1 TYR A 248 86.017 28.034 −0.067 1.00 15.65 A ATOM 1337 CD2 TYR A 248 83.820 28.784 1.460 1.00 13.57 A ATOM 1338 CE2 TYR A 248 85.086 28.757 2.039 1.00 13.28 A ATOM 1339 CZ TYR A 248 86.192 28.386 1.271 1.00 16.78 A ATOM 1340 OH TYR A 248 87.471 28.411 1.816 1.00 15.10 A ATOM 1341 C TYR A 248 80.827 30.091 −2.005 1.00 22.23 A ATOM 1342 O TYR A 248 80.523 29.268 −2.866 1.00 22.78 A ATOM 1343 N VAL A 249 80.054 31.126 −1.680 1.00 21.81 A ATOM 1344 CA VAL A 249 78.760 31.395 −2.308 1.00 22.22 A ATOM 1345 CB VAL A 249 78.077 32.634 −1.640 1.00 22.82 A ATOM 1346 CG1 VAL A 249 76.904 33.139 −2.496 1.00 22.57 A ATOM 1347 CG2 VAL A 249 77.606 32.270 −0.243 1.00 22.62 A ATOM 1348 C VAL A 249 78.878 31.666 −3.818 1.00 21.92 A ATOM 1349 O VAL A 249 79.733 32.428 −4.255 1.00 20.01 A ATOM 1350 N SER A 250 78.012 31.045 −4.609 1.00 22.88 A ATOM 1351 CA SER A 250 78.030 31.259 −6.049 1.00 24.81 A ATOM 1352 CB SER A 250 77.357 30.105 −6.792 1.00 25.82 A ATOM 1353 OG SER A 250 75.999 29.984 −6.419 1.00 27.07 A ATOM 1354 C SER A 250 77.288 32.546 −6.357 1.00 26.22 A ATOM 1355 O SER A 250 76.438 33.004 −5.582 1.00 25.88 A ATOM 1356 N PRO A 251 77.592 33.148 −7.506 1.00 26.70 A ATOM 1357 CD PRO A 251 78.632 32.813 −8.495 1.00 27.24 A ATOM 1358 CA PRO A 251 76.908 34.393 −7.847 1.00 27.08 A ATOM 1359 CB PRO A 251 77.637 34.860 −9.113 1.00 25.51 A ATOM 1360 CG PRO A 251 78.171 33.590 −9.701 1.00 27.43 A ATOM 1361 C PRO A 251 75.399 34.288 −8.026 1.00 28.00 A ATOM 1362 O PRO A 251 74.684 35.218 −7.678 1.00 28.30 A ATOM 1363 N GLU A 252 74.908 33.166 −8.550 1.00 28.81 A ATOM 1364 CA GLU A 252 73.469 33.012 −8.768 1.00 29.67 A ATOM 1365 CB GLU A 252 73.151 31.684 −9.463 1.00 29.72 A ATOM 1366 CG GLU A 252 73.698 30.453 −8.740 1.00 31.04 A ATOM 1367 CD GLU A 252 75.106 30.075 −9.191 1.00 30.61 A ATOM 1368 OE1 GLU A 252 75.880 30.973 −9.597 1.00 30.55 A ATOM 1369 OE2 GLU A 252 75.434 28.872 −9.130 1.00 30.80 A ATOM 1370 C GLU A 252 72.709 33.083 −7.462 1.00 30.83 A ATOM 1371 O GLU A 252 71.563 33.530 −7.423 1.00 31.87 A ATOM 1372 N LEU A 253 73.351 32.639 −6.388 1.00 32.71 A ATOM 1373 CA LEU A 253 72.734 32.655 −5.073 1.00 33.94 A ATOM 1374 CB LEU A 253 73.612 31.901 −4.081 1.00 37.40 A ATOM 1375 CG LEU A 253 72.967 31.086 −2.950 1.00 41.64 A ATOM 1376 CD1 LEU A 253 72.067 31.925 −2.048 1.00 43.86 A ATOM 1377 CD2 LEU A 253 72.144 30.017 −3.597 1.00 45.52 A ATOM 1378 C LEU A 253 72.545 34.095 −4.603 1.00 35.67 A ATOM 1379 O LEU A 253 71.589 34.392 −3.897 1.00 37.48 A ATOM 1380 N LEU A 254 73.451 34.989 −4.995 1.00 36.38 A ATOM 1381 CA LEU A 254 73.372 36.397 −4.600 1.00 36.66 A ATOM 1382 CB LEU A 254 74.764 37.032 −4.572 1.00 33.81 A ATOM 1383 CG LEU A 254 75.824 36.402 −3.674 1.00 33.40 A ATOM 1384 CD1 LEU A 254 77.183 37.022 −3.982 1.00 30.48 A ATOM 1385 CD2 LEU A 254 75.440 36.574 −2.208 1.00 31.43 A ATOM 1386 C LEU A 254 72.485 37.240 −5.511 1.00 38.89 A ATOM 1387 O LEU A 254 72.079 38.328 −5.133 1.00 38.85 A ATOM 1388 N THR A 255 72.187 36.754 −6.709 1.00 42.60 A ATOM 1389 CA THR A 255 71.358 37.528 −7.624 1.00 47.21 A ATOM 1390 CB THR A 255 72.102 37.847 −8.941 1.00 47.08 A ATOM 1391 OG1 THR A 255 72.008 36.718 −9.814 1.00 48.56 A ATOM 1392 CG2 THR A 255 73.581 38.157 −8.686 1.00 45.65 A ATOM 1393 C THR A 255 70.044 36.848 −8.009 1.00 51.00 A ATOM 1394 O THR A 255 69.348 37.323 −8.903 1.00 51.80 A ATOM 1395 N GLU A 256 69.696 35.745 −7.353 1.00 55.01 A ATOM 1396 CA GLU A 256 68.450 35.044 −7.683 1.00 58.97 A ATOM 1397 CB GLU A 256 68.679 34.057 −8.832 1.00 59.81 A ATOM 1398 CG GLU A 256 68.922 34.707 −10.181 1.00 63.59 A ATOM 1399 CD GLU A 256 69.343 33.707 −11.240 1.00 65.64 A ATOM 1400 OE1 GLU A 256 68.727 32.617 −11.310 1.00 67.44 A ATOM 1401 OE2 GLU A 256 70.285 34.015 −12.007 1.00 66.61 A ATOM 1402 C GLU A 256 67.859 34.279 −6.512 1.00 60.83 A ATOM 1403 O GLU A 256 66.701 33.861 −6.563 1.00 61.27 A ATOM 1404 N ALA A 257 68.657 34.100 −5.463 1.00 62.31 A ATOM 1405 CA ALA A 257 68.234 33.348 −4.285 1.00 63.29 A ATOM 1406 CB ALA A 257 66.867 33.847 −3.784 1.00 62.76 A ATOM 1407 C ALA A 257 68.157 31.860 −4.651 1.00 63.64 A ATOM 1408 O ALA A 257 67.790 31.028 −3.825 1.00 64.96 A ATOM 1409 N SER A 258 68.523 31.532 −5.888 1.00 62.79 A ATOM 1410 CA SER A 258 68.485 30.150 −6.378 1.00 62.30 A ATOM 1411 CB SER A 258 68.049 30.144 −7.847 1.00 63.00 A ATOM 1412 OG SER A 258 68.762 31.129 −8.582 1.00 63.40 A ATOM 1413 C SER A 258 69.816 29.402 −6.237 1.00 61.09 A ATOM 1414 O SER A 258 70.862 30.009 −6.009 1.00 62.12 A ATOM 1415 N ALA A 259 69.774 28.083 −6.389 1.00 58.47 A ATOM 1416 CA ALA A 259 70.979 27.270 −6.278 1.00 55.79 A ATOM 1417 CB ALA A 259 71.403 27.164 −4.837 1.00 56.24 A ATOM 1418 C ALA A 259 70.738 25.886 −6.842 1.00 53.38 A ATOM 1419 O ALA A 259 69.641 25.347 −6.736 1.00 54.10 A ATOM 1420 N CYS A 260 71.768 25.30 −7.433 1.00 49.75 A ATOM 1421 CA CYS A 260 71.623 23.988 −8.015 1.00 45.68 A ATOM 1422 CB CYS A 260 71.067 24.106 −9.438 1.00 48.50 A ATOM 1423 SG CYS A 260 69.936 22.732 −9.899 1.00 57.53 A ATOM 1424 C CYS A 260 72.980 23.318 −8.022 1.00 41.30 A ATOM 1425 O CYS A 260 73.892 23.762 −7.335 1.00 39.24 A ATOM 1426 N LYS A 261 73.118 22.258 −8.805 1.00 36.63 A ATOM 1427 CA LYS A 261 74.369 21.535 −8.866 1.00 33.81 A ATOM 1428 CB LYS A 261 74.261 20.416 −9.897 1.00 34.27 A ATOM 1429 CG LYS A 261 73.250 19.362 −9.488 1.00 34.04 A ATOM 1430 CD LYS A 261 72.995 18.353 −10.577 1.00 33.10 A ATOM 1431 CE LYS A 261 71.983 17.336 −10.105 1.00 32.48 A ATOM 1432 NZ LYS A 261 71.660 16.357 −11.176 1.00 33.10 A ATOM 1433 C LYS A 261 75.565 22.419 −9.153 1.00 31.80 A ATOM 1434 O LYS A 261 76.636 22.214 −8.589 1.00 31.89 A ATOM 1435 N SER A 262 75.389 23.405 −10.025 1.00 29.92 A ATOM 1436 CA SER A 262 76.477 24.314 −10.354 1.00 28.19 A ATOM 1437 CB SER A 262 76.034 25.309 −11.417 1.00 29.90 A ATOM 1438 OG SER A 262 76.184 24.732 −12.695 1.00 34.45 A ATOM 1439 C SER A 262 77.047 25.069 −9.155 1.00 25.77 A ATOM 1440 O SER A 262 78.225 25.405 −9.146 1.00 26.59 A ATOM 1441 N SER A 263 76.216 25.347 −8.159 1.00 23.42 A ATOM 1442 CA SER A 263 76.663 26.040 −6.953 1.00 23.04 A ATOM 1443 CB SER A 263 75.502 26.209 −5.979 1.00 24.64 A ATOM 1444 OG SER A 263 74.463 26.963 −6.572 1.00 31.12 A ATOM 1445 C SER A 263 77.777 25.233 −6.283 1.00 21.37 A ATOM 1446 O SER A 263 78.745 25.803 −5.788 1.00 20.74 A ATOM 1447 N ASP A 264 77.640 23.909 −6.268 1.00 19.11 A ATOM 1448 CA ASP A 264 78.674 23.06 −5.682 1.00 19.35 A ATOM 1449 CB ASP A 264 78.206 21.609 −5.579 1.00 18.45 A ATOM 1450 CG ASP A 264 77.164 21.406 −4.500 1.00 19.39 A ATOM 1451 OD1 ASP A 264 76.998 22.304 −3.649 1.00 20.34 A ATOM 1452 OD2 ASP A 264 76.522 20.338 −4.488 1.00 19.48 A ATOM 1453 C ASP A 264 79.943 23.127 −6.542 1.00 19.34 A ATOM 1454 O ASP A 264 81.052 23.147 −6.018 1.00 20.70 A ATOM 1455 N LEU A 265 79.772 23.16 −7.864 1.00 17.68 A ATOM 1456 CA LEU A 265 80.898 23.23 −8.774 1.00 17.42 A ATOM 1457 CB LEU A 265 80.406 23.058 −10.208 1.00 19.36 A ATOM 1458 CG LEU A 265 79.683 21.717 −10.453 1.00 19.53 A ATOM 1459 CD1 LEU A 265 79.189 21.655 −11.879 1.00 17.18 A ATOM 1460 CD2 LEU A 265 80.625 20.550 −10.168 1.00 14.91 A ATOM 1461 C LEU A 265 81.619 24.566 −8.600 1.00 19.06 A ATOM 1462 O LEU A 265 82.850 24.649 −8.697 1.00 18.60 A ATOM 1463 N TRP A 266 80.853 25.621 −8.350 1.00 18.60 A ATOM 1464 CA TRP A 266 81.468 26.902 −8.107 1.00 18.62 A ATOM 1465 CB TRP A 266 80.405 27.976 −7.876 1.00 19.75 A ATOM 1466 CG TRP A 266 80.997 29.277 −7.382 1.00 21.53 A ATOM 1467 CD2 TRP A 266 81.357 30.420 −8.174 1.00 22.40 A ATOM 1468 CE2 TRP A 266 81.917 31.375 −7.296 1.00 22.70 A ATOM 1469 CE3 TRP A 266 81.260 30.728 −9.541 1.00 21.62 A ATOM 1470 CD1 TRP A 266 81.344 29.582 −6.094 1.00 20.15 A ATOM 1471 NE1 TRP A 266 81.896 30.835 −6.037 1.00 20.80 A ATOM 1472 CZ2 TRP A 266 82.382 32.624 −7.739 1.00 22.47 A ATOM 1473 CZ3 TRP A 266 81.721 31.961 −9.981 1.00 22.48 A ATOM 1474 CH2 TRP A 266 82.276 32.898 −9.080 1.00 23.40 A ATOM 1475 C TRP A 266 82.338 26.734 −6.857 1.00 18.89 A ATOM 1476 O TRP A 266 83.523 27.070 −6.875 1.00 20.01 A ATOM 1477 N ALA A 267 81.755 26.204 −5.780 1.00 16.09 A ATOM 1478 CA ALA A 267 82.502 25.994 −4.540 1.00 15.55 A ATOM 1479 CB ALA A 267 81.630 25.313 −3.499 1.00 13.20 A ATOM 1480 C ALA A 267 83.738 25.145 −4.813 1.00 16.44 A ATOM 1481 O ALA A 267 84.802 25.345 −4.218 1.00 17.65 A ATOM 1482 N LEU A 268 83.597 24.181 −5.710 1.00 15.96 A ATOM 1483 CA LEU A 268 84.732 23.336 −6.055 1.00 17.56 A ATOM 1484 CB LEU A 268 84.315 22.281 −7.098 1.00 16.91 A ATOM 1485 CG LEU A 268 85.477 21.535 −7.775 1.00 16.43 A ATOM 1486 CD1 LEU A 268 86.214 20.697 −6.766 1.00 15.17 A ATOM 1487 CD2 LEU A 268 84.947 20.643 −8.871 1.00 17.18 A ATOM 1488 C LEU A 268 85.892 24.193 −6.599 1.00 15.96 A ATOM 1489 O LEU A 268 87.032 24.040 −6.178 1.00 14.54 A ATOM 1490 N GLY A 269 85.578 25.092 −7.530 1.00 17.15 A ATOM 1491 CA GLY A 269 86.590 25.957 −8.116 1.00 18.32 A ATOM 1492 C GLY A 269 87.339 26.722 −7.042 1.00 19.39 A ATOM 1493 O GLY A 269 88.579 26.777 −7.042 1.00 19.66 A ATOM 1494 N CYS A 270 86.579 27.297 −6.111 1.00 17.50 A ATOM 1495 CA CYS A 270 87.154 28.043 −5.010 1.00 17.72 A ATOM 1496 CB CYS A 270 86.047 28.551 −4.088 1.00 18.96 A ATOM 1497 SG CYS A 270 84.981 29.801 −4.798 1.00 19.62 A ATOM 1498 C CYS A 270 88.114 27.182 −4.201 1.00 18.63 A ATOM 1499 O CYS A 270 89.213 27.612 −3.850 1.00 18.78 A ATOM 1500 N ILE A 271 87.679 25.962 −3.900 1.00 20.05 A ATOM 1501 CA ILE A 271 88.479 25.019 −3.130 1.00 20.08 A ATOM 1502 CB ILE A 271 87.668 23.755 −2.812 1.00 20.09 A ATOM 1503 CG2 ILE A 271 88.592 22.654 −2.302 1.00 18.31 A ATOM 1504 CG1 ILE A 271 86.558 24.104 −1.810 1.00 18.38 A ATOM 1505 CD1 ILE A 271 85.396 23.125 −1.783 1.00 14.68 A ATOM 1506 C ILE A 271 89.761 24.629 −3.858 1.00 20.41 A ATOM 1507 O ILE A 271 90.826 24.548 −3.234 1.00 21.81 A ATOM 1508 N ILE A 272 89.669 24.398 −5.166 1.00 18.41 A ATOM 1509 CA ILE A 272 90.860 24.035 −5.934 1.00 19.20 A ATOM 1510 CB ILE A 272 90.526 23.730 −7.412 1.00 20.04 A ATOM 1511 CG2 ILE A 272 91.808 23.488 −8.199 1.00 17.73 A ATOM 1512 CG1 ILE A 272 89.602 22.523 −7.513 1.00 19.47 A ATOM 1513 CD1 ILE A 272 89.001 22.386 −8.872 1.00 20.31 A ATOM 1514 C ILE A 272 91.858 25.191 −5.932 1.00 19.57 A ATOM 1515 O ILE A 272 93.061 24.978 −5.884 1.00 20.97 A ATOM 1516 N TYR A 273 91.338 26.413 −6.028 1.00 19.42 A ATOM 1517 CA TYR A 273 92.157 27.606 −6.041 1.00 18.41 A ATOM 1518 CB TYR A 273 91.272 28.826 −6.294 1.00 18.70 A ATOM 1519 CG TYR A 273 91.998 30.147 −6.252 1.00 19.81 A ATOM 1520 CD1 TYR A 273 92.357 30.729 −5.035 1.00 21.25 A ATOM 1521 CE1 TYR A 273 93.072 31.936 −4.990 1.00 22.12 A ATOM 1522 CD2 TYR A 273 92.366 30.804 −7.433 1.00 20.45 A ATOM 1523 CE2 TYR A 273 93.081 32.005 −7.403 1.00 20.42 A ATOM 1524 CZ TYR A 273 93.432 32.563 −6.178 1.00 23.33 A ATOM 1525 OH TYR A 273 94.159 33.731 −6.138 1.00 23.26 A ATOM 1526 C TYR A 273 92.848 27.699 −4.687 1.00 19.40 A ATOM 1527 O TYR A 273 94.051 27.945 −4.598 1.00 19.44 A ATOM 1528 N GLN A 274 92.079 27.471 −3.632 1.00 19.53 A ATOM 1529 CA GLN A 274 92.602 27.517 −2.278 1.00 21.26 A ATOM 1530 CB GLN A 274 91.450 27.399 −1.290 1.00 22.36 A ATOM 1531 CG GLN A 274 91.838 27.629 0.142 1.00 21.87 A ATOM 1532 CD GLN A 274 90.643 27.531 1.054 1.00 23.64 A ATOM 1533 OE1 GLN A 274 89.499 27.479 0.585 1.00 22.12 A ATOM 1534 NE2 GLN A 274 90.890 27.517 2.369 1.00 24.45 A ATOM 1535 C GLN A 274 93.656 26.435 −1.980 1.00 22.20 A ATOM 1536 O GLN A 274 94.549 26.652 −1.160 1.00 22.03 A ATOM 1537 N LEU A 275 93.558 25.275 −2.625 1.00 21.82 A ATOM 1538 CA LEU A 275 94.550 24.223 −2.385 1.00 21.95 A ATOM 1539 CB LEU A 275 94.104 22.886 −3.015 1.00 19.19 A ATOM 1540 CG LEU A 275 92.934 22.153 −2.341 1.00 19.86 A ATOM 1541 CD1 LEU A 275 92.528 20.915 −3.134 1.00 19.79 A ATOM 1542 CD2 LEU A 275 93.333 21.757 −0.938 1.00 16.56 A ATOM 1543 C LEU A 275 95.910 24.630 −2.962 1.00 21.62 A ATOM 1544 O LEU A 275 96.950 24.414 −2.353 1.00 21.98 A ATOM 1545 N VAL A 276 95.884 25.239 −4.137 1.00 20.54 A ATOM 1546 CA VAL A 276 97.095 25.639 −4.828 1.00 21.48 A ATOM 1547 CB VAL A 276 96.810 25.795 −6.338 1.00 21.76 A ATOM 1548 CG1 VAL A 276 98.035 26.269 −7.061 1.00 20.72 A ATOM 1549 CG2 VAL A 276 96.332 24.479 −6.908 1.00 21.98 A ATOM 1550 C VAL A 276 97.696 26.946 −4.315 1.00 23.17 A ATOM 1551 O VAL A 276 98.913 27.055 −4.141 1.00 24.82 A ATOM 1552 N ALA A 277 96.837 27.934 −4.085 1.00 22.20 A ATOM 1553 CA ALA A 277 97.271 29.230 −3.628 1.00 19.31 A ATOM 1554 CB ALA A 277 96.339 30.293 −4.174 1.00 19.24 A ATOM 1555 C ALA A 277 97.380 29.350 −2.113 1.00 20.10 A ATOM 1556 O ALA A 277 98.096 30.222 −1.622 1.00 20.73 A ATOM 1557 N GLY A 278 96.686 28.493 −1.368 1.00 19.16 A ATOM 1558 CA GLY A 278 96.748 28.579 0.084 1.00 18.62 A ATOM 1559 C GLY A 278 95.634 29.425 0.677 1.00 21.09 A ATOM 1560 O GLY A 278 95.462 29.483 1.903 1.00 20.36 A ATOM 1561 N LEU A 279 94.865 30.084 −0.190 1.00 22.58 A ATOM 1562 CA LEU A 279 93.742 30.917 0.254 1.00 24.03 A ATOM 1563 CB LEU A 279 94.190 32.365 0.448 1.00 23.98 A ATOM 1564 CG LEU A 279 95.322 32.744 1.396 1.00 25.93 A ATOM 1565 CD1 LEU A 279 95.622 34.215 1.140 1.00 25.95 A ATOM 1566 CD2 LEU A 279 94.950 32.511 2.873 1.00 24.23 A ATOM 1567 C LEU A 279 92.575 30.940 −0.735 1.00 23.96 A ATOM 1568 O LEU A 279 92.759 30.776 −1.939 1.00 23.93 A ATOM 1569 N PRO A 280 91.353 31.151 −0.231 1.00 24.60 A ATOM 1570 CD PRO A 280 90.987 31.360 1.185 1.00 23.93 A ATOM 1571 CA PRO A 280 90.177 31.208 −1.109 1.00 24.56 A ATOM 1572 CB PRO A 280 89.024 31.319 −0.116 1.00 24.33 A ATOM 1573 CG PRO A 280 89.656 32.027 1.076 1.00 24.23 A ATOM 1574 C PRO A 280 90.324 32.453 −2.033 1.00 25.82 A ATOM 1575 O PRO A 280 90.892 33.458 −1.632 1.00 27.28 A ATOM 1576 N PRO A 281 89.798 32.396 −3.268 1.00 25.40 A ATOM 1577 CD PRO A 281 88.807 31.385 −3.660 1.00 26.04 A ATOM 1578 CA PRO A 281 89.862 33.470 −4.272 1.00 24.99 A ATOM 1579 CB PRO A 281 89.150 32.871 −5.489 1.00 24.76 A ATOM 1580 CG PRO A 281 88.882 31.442 −5.137 1.00 26.48 A ATOM 1581 C PRO A 281 89.254 34.836 −3.921 1.00 25.24 A ATOM 1582 O PRO A 281 89.803 35.886 −4.272 1.00 25.07 A ATOM 1583 N PHE A 282 88.103 34.821 −3.264 1.00 24.47 A ATOM 1584 CA PHE A 282 87.435 36.059 −2.918 1.00 24.29 A ATOM 1585 CB PHE A 282 85.964 35.961 −3.320 1.00 23.11 A ATOM 1586 CG PHE A 282 85.759 35.596 −4.774 1.00 21.99 A ATOM 1587 CD1 PHE A 282 85.936 36.543 −5.775 1.00 20.97 A ATOM 1588 CD2 PHE A 282 85.448 34.285 −5.139 1.00 21.76 A ATOM 1589 CE1 PHE A 282 85.812 36.194 −7.124 1.00 20.59 A ATOM 1590 CE2 PHE A 282 85.325 33.923 −6.469 1.00 20.98 A ATOM 1591 CZ PHE A 282 85.509 34.885 −7.471 1.00 23.01 A ATOM 1592 C PHE A 282 87.579 36.366 −1.435 1.00 25.85 A ATOM 1593 O PHE A 282 86.963 35.707 −0.596 1.00 27.04 A ATOM 1594 N ARG A 283 88.414 37.358 −1.124 1.00 27.56 A ATOM 1595 CA ARG A 283 88.676 37.784 0.260 1.00 27.41 A ATOM 1596 CB ARG A 283 90.116 37.451 0.648 1.00 28.05 A ATOM 1597 CG ARG A 283 90.523 36.020 0.327 1.00 32.73 A ATOM 1598 CD ARG A 283 91.944 35.722 0.788 1.00 36.54 A ATOM 1599 NE ARG A 283 92.942 36.490 0.043 1.00 39.92 A ATOM 1600 CZ ARG A 283 93.202 36.329 −1.253 1.00 42.59 A ATOM 1601 NH1 ARG A 283 92.544 35.421 −1.961 1.00 44.54 A ATOM 1602 NH2 ARG A 283 94.112 37.090 −1.853 1.00 43.94 A ATOM 1603 C ARG A 283 88.445 39.291 0.394 1.00 27.01 A ATOM 1604 O ARG A 283 88.682 40.047 −0.557 1.00 26.54 A ATOM 1605 N ALA A 284 87.977 39.724 1.568 1.00 26.05 A ATOM 1606 CA ALA A 284 87.694 41.135 1.812 1.00 23.42 A ATOM 1607 CB ALA A 284 86.529 41.579 0.967 1.00 21.82 A ATOM 1608 C ALA A 284 87.386 41.383 3.280 1.00 24.72 A ATOM 1609 O ALA A 284 87.193 40.440 4.048 1.00 24.83 A ATOM 1610 N GLY A 285 87.330 42.663 3.659 1.00 25.04 A ATOM 1611 CA GLY A 285 87.055 43.039 5.035 1.00 23.67 A ATOM 1612 C GLY A 285 85.761 42.542 5.652 1.00 25.13 A ATOM 1613 O GLY A 285 85.718 42.302 6.855 1.00 26.60 A ATOM 1614 N ASN A 286 84.700 42.399 4.862 1.00 24.84 A ATOM 1615 CA ASN A 286 83.418 41.923 5.391 1.00 23.82 A ATOM 1616 CB ASN A 286 82.567 43.098 5.899 1.00 23.66 A ATOM 1617 CG ASN A 286 82.362 44.190 4.843 1.00 24.14 A ATOM 1618 OD1 ASN A 286 81.835 43.947 3.747 1.00 22.27 A ATOM 1619 ND2 ASN A 286 82.776 45.402 5.178 1.00 24.49 A ATOM 1620 C ASN A 286 82.672 41.185 4.296 1.00 24.75 A ATOM 1621 O ASN A 286 83.124 41.160 3.153 1.00 25.32 A ATOM 1622 N GLU A 287 81.522 40.610 4.630 1.00 26.04 A ATOM 1623 CA GLU A 287 80.746 39.865 3.641 1.00 27.47 A ATOM 1624 CB GLU A 287 79.549 39.175 4.287 1.00 30.33 A ATOM 1625 CG GLU A 287 79.935 38.202 5.364 1.00 36.51 A ATOM 1626 CD GLU A 287 78.792 37.288 5.766 1.00 41.45 A ATOM 1627 OE1 GLU A 287 77.608 37.712 5.641 1.00 43.02 A ATOM 1628 OE2 GLU A 287 79.092 36.155 6.222 1.00 41.33 A ATOM 1629 C GLU A 287 80.250 40.679 2.467 1.00 25.95 A ATOM 1630 O GLU A 287 80.279 40.203 1.330 1.00 25.67 A ATOM 1631 N TYR A 288 79.772 41.893 2.730 1.00 25.20 A ATOM 1632 CA TYR A 288 79.276 42.731 1.644 1.00 22.91 A ATOM 1633 CB TYR A 288 78.870 44.113 2.152 1.00 22.98 A ATOM 1634 CG TYR A 288 78.459 45.068 1.038 1.00 23.01 A ATOM 1635 CD1 TYR A 288 77.166 45.031 0.478 1.00 24.16 A ATOM 1636 CE1 TYR A 288 76.814 45.869 −0.589 1.00 22.73 A ATOM 1637 CD2 TYR A 288 79.376 45.965 0.508 1.00 21.34 A ATOM 1638 CE2 TYR A 288 79.043 46.796 −0.551 1.00 23.71 A ATOM 1639 CZ TYR A 288 77.771 46.748 −1.099 1.00 25.48 A ATOM 1640 OH TYR A 288 77.490 47.571 −2.172 1.00 26.98 A ATOM 1641 C TYR A 288 80.352 42.882 0.578 1.00 22.37 A ATOM 1642 O TYR A 288 80.068 42.735 −0.603 1.00 22.65 A ATOM 1643 N LEU A 289 81.590 43.155 0.993 1.00 22.04 A ATOM 1644 CA LEU A 289 82.691 43.326 0.037 1.00 23.92 A ATOM 1645 CB LEU A 289 83.927 43.907 0.748 1.00 21.71 A ATOM 1646 CG LEU A 289 83.661 45.326 1.298 1.00 23.89 A ATOM 1647 CD1 LEU A 289 84.716 45.787 2.326 1.00 17.24 A ATOM 1648 CD2 LEU A 289 83.570 46.273 0.118 1.00 19.08 A ATOM 1649 C LEU A 289 83.050 42.025 −0.693 1.00 24.50 A ATOM 1650 O LEU A 289 83.446 42.042 −1.852 1.00 24.85 A ATOM 1651 N ILE A 290 82.906 40.904 −0.002 1.00 24.71 A ATOM 1652 CA ILE A 290 83.182 39.601 −0.570 1.00 25.86 A ATOM 1653 CB ILE A 290 83.131 38.521 0.528 1.00 26.67 A ATOM 1654 CG2 ILE A 290 83.229 37.154 −0.087 1.00 27.57 A ATOM 1655 CG1 ILE A 290 84.282 38.736 1.511 1.00 28.90 A ATOM 1656 CD1 ILE A 290 84.173 37.928 2.798 1.00 28.83 A ATOM 1657 C ILE A 290 82.127 39.303 −1.637 1.00 26.89 A ATOM 1658 O ILE A 290 82.446 38.879 −2.757 1.00 26.18 A ATOM 1659 N PHE A 291 80.864 39.531 −1.294 1.00 27.48 A ATOM 1660 CA PHE A 291 79.789 39.287 −2.249 1.00 28.46 A ATOM 1661 CB PHE A 291 78.434 39.587 −1.620 1.00 27.24 A ATOM 1662 CG PHE A 291 78.079 38.664 −0.496 1.00 27.02 A ATOM 1663 CD1 PHE A 291 78.716 37.431 −0.365 1.00 26.90 A ATOM 1664 CD2 PHE A 291 77.074 38.996 0.399 1.00 25.83 A ATOM 1665 CE1 PHE A 291 78.353 36.545 0.637 1.00 27.02 A ATOM 1666 CE2 PHE A 291 76.700 38.109 1.412 1.00 28.02 A ATOM 1667 CZ PHE A 291 77.338 36.882 1.532 1.00 26.74 A ATOM 1668 C PHE A 291 79.971 40.159 −3.467 1.00 29.11 A ATOM 1669 O PHE A 291 79.595 39.787 −4.584 1.00 30.18 A ATOM 1670 N GLN A 292 80.559 41.324 −3.240 1.00 28.88 A ATOM 1671 CA GLN A 292 80.783 42.280 −4.304 1.00 30.00 A ATOM 1672 CB GLN A 292 81.215 43.604 −3.679 1.00 32.57 A ATOM 1673 CG GLN A 292 81.191 44.799 −4.599 1.00 35.12 A ATOM 1674 CD GLN A 292 81.208 46.113 −3.817 1.00 38.65 A ATOM 1675 OE1 GLN A 292 82.159 46.409 −3.078 1.00 39.67 A ATOM 1676 NE2 GLN A 292 80.150 46.903 −3.972 1.00 38.94 A ATOM 1677 C GLN A 292 81.822 41.755 −5.296 1.00 28.96 A ATOM 1678 O GLN A 292 81.633 41.844 −6.510 1.00 28.45 A ATOM 1679 N LYS A 293 82.910 41.193 −4.787 1.00 26.32 A ATOM 1680 CA LYS A 293 83.930 40.661 −5.669 1.00 26.90 A ATOM 1681 CB LYS A 293 85.174 40.319 −4.858 1.00 28.03 A ATOM 1682 CG LYS A 293 85.777 41.539 −4.177 1.00 28.52 A ATOM 1683 CD LYS A 293 87.065 41.208 −3.482 1.00 29.14 A ATOM 1684 CE LYS A 293 87.912 42.449 −3.269 1.00 30.09 A ATOM 1685 NZ LYS A 293 89.165 42.157 −2.490 1.00 30.06 A ATOM 1686 C LYS A 293 83.414 39.432 −6.434 1.00 26.13 A ATOM 1687 O LYS A 293 83.721 39.231 −7.617 1.00 26.02 A ATOM 1688 N ILE A 294 82.617 38.621 −5.755 1.00 24.49 A ATOM 1689 CA ILE A 294 82.047 37.429 −6.362 1.00 24.40 A ATOM 1690 CB ILE A 294 81.168 36.680 −5.340 1.00 23.24 A ATOM 1691 CG2 ILE A 294 80.154 35.763 −6.046 1.00 21.00 A ATOM 1692 CG1 ILE A 294 82.072 35.929 −4.365 1.00 19.23 A ATOM 1693 CD1 ILE A 294 81.388 35.559 −3.067 1.00 17.91 A ATOM 1694 C ILE A 294 81.224 37.744 −7.608 1.00 26.38 A ATOM 1695 O ILE A 294 81.428 37.139 −8.661 1.00 25.96 A ATOM 1696 N ILE A 295 80.303 38.694 −7.505 1.00 28.38 A ATOM 1697 CA ILE A 295 79.467 39.018 −8.659 1.00 31.11 A ATOM 1698 CB ILE A 295 78.243 39.852 −8.248 1.00 31.46 A ATOM 1699 CG2 ILE A 295 77.548 39.181 −7.068 1.00 32.78 A ATOM 1700 CG1 ILE A 295 78.669 41.268 −7.871 1.00 31.79 A ATOM 1701 CD1 ILE A 295 77.518 42.132 −7.438 1.00 33.46 A ATOM 1702 C ILE A 295 80.201 39.731 −9.798 1.00 31.35 A ATOM 1703 O ILE A 295 79.709 39.784 −10.930 1.00 32.03 A ATOM 1704 N LYS A 296 81.374 40.269 −9.511 1.00 30.68 A ATOM 1705 CA LYS A 296 82.129 40.937 −10.552 1.00 31.64 A ATOM 1706 CB LYS A 296 82.683 42.275 −10.041 1.00 32.01 A ATOM 1707 CG LYS A 296 81.605 43.213 −9.520 1.00 34.12 A ATOM 1708 CD LYS A 296 82.184 44.441 −8.841 1.00 37.38 A ATOM 1709 CE LYS A 296 82.299 45.609 −9.803 1.00 40.30 A ATOM 1710 NZ LYS A 296 82.864 46.819 −9.119 1.00 42.94 A ATOM 1711 C LYS A 296 83.258 40.010 −10.966 1.00 31.87 A ATOM 1712 O LYS A 296 84.135 40.398 −11.745 1.00 32.98 A ATOM 1713 N LEU A 297 83.227 38.780 −10.443 1.00 30.62 A ATOM 1714 CA LEU A 297 84.253 37.775 −10.735 1.00 29.78 A ATOM 1715 CB LEU A 297 84.100 37.253 −12.169 1.00 29.42 A ATOM 1716 CG LEU A 297 84.802 35.931 −12.527 1.00 29.13 A ATOM 1717 CD1 LEU A 297 84.142 34.776 −11.783 1.00 27.91 A ATOM 1718 CD2 LEU A 297 84.725 35.682 −14.024 1.00 26.86 A ATOM 1719 C LEU A 297 85.622 38.436 −10.565 1.00 29.62 A ATOM 1720 O LEU A 297 86.489 38.333 −11.419 1.00 28.99 A ATOM 1721 N GLU A 298 85.807 39.091 −9.427 1.00 29.81 A ATOM 1722 CA GLU A 298 87.027 39.826 −9.143 1.00 30.88 A ATOM 1723 CB GLU A 298 86.622 41.166 −8.510 1.00 33.22 A ATOM 1724 CG GLU A 298 87.754 42.136 −8.228 1.00 38.19 A ATOM 1725 CD GLU A 298 87.317 43.274 −7.303 1.00 41.34 A ATOM 1726 OE1 GLU A 298 86.416 44.054 −7.684 1.00 43.93 A ATOM 1727 OE2 GLU A 298 87.867 43.382 −6.187 1.00 43.19 A ATOM 1728 C GLU A 298 88.071 39.110 −8.269 1.00 29.28 A ATOM 1729 O GLU A 298 88.066 39.230 −7.045 1.00 30.04 A ATOM 1730 N TYR A 299 88.972 38.375 −8.906 1.00 26.46 A ATOM 1731 CA TYR A 299 90.034 37.669 −8.194 1.00 26.46 A ATOM 1732 CB TYR A 299 89.548 36.315 −7.640 1.00 24.23 A ATOM 1733 CG TYR A 299 89.403 35.252 −8.709 1.00 23.32 A ATOM 1734 CD1 TYR A 299 88.369 35.318 −9.653 1.00 23.42 A ATOM 1735 CE1 TYR A 299 88.274 34.392 −10.686 1.00 23.13 A ATOM 1736 CD2 TYR A 299 90.337 34.227 −8.829 1.00 21.77 A ATOM 1737 CE2 TYR A 299 90.250 33.292 −9.864 1.00 21.81 A ATOM 1738 CZ TYR A 299 89.214 33.379 −10.784 1.00 22.35 A ATOM 1739 OH TYR A 299 89.089 32.444 −11.780 1.00 21.61 A ATOM 1740 C TYR A 299 91.102 37.416 −9.245 1.00 28.31 A ATOM 1741 O TYR A 299 90.864 37.622 −10.426 1.00 27.25 A ATOM 1742 N ASP A 300 92.277 36.959 −8.844 1.00 30.57 A ATOM 1743 CA ASP A 300 93.282 36.687 −9.851 1.00 33.57 A ATOM 1744 CB ASP A 300 94.012 37.980 −10.193 1.00 38.77 A ATOM 1745 CG ASP A 300 94.382 38.768 −8.968 1.00 43.17 A ATOM 1746 OD1 ASP A 300 95.245 38.283 −8.197 1.00 46.59 A ATOM 1747 OD2 ASP A 300 93.802 39.865 −8.773 1.00 45.78 A ATOM 1748 C ASP A 300 94.232 35.607 −9.364 1.00 33.20 A ATOM 1749 O ASP A 300 94.311 35.354 −8.169 1.00 33.46 A ATOM 1750 N PHE A 301 94.937 34.959 −10.287 1.00 32.16 A ATOM 1751 CA PHE A 301 95.853 33.892 −9.910 1.00 33.41 A ATOM 1752 CB PHE A 301 95.922 32.813 −11.001 1.00 32.89 A ATOM 1753 CG PHE A 301 94.590 32.240 −11.403 1.00 33.05 A ATOM 1754 CD1 PHE A 301 93.763 32.921 −12.297 1.00 31.61 A ATOM 1755 CD2 PHE A 301 94.171 31.006 −10.905 1.00 30.94 A ATOM 1756 CE1 PHE A 301 92.548 32.387 −12.687 1.00 31.29 A ATOM 1757 CE2 PHE A 301 92.961 30.466 −11.287 1.00 31.42 A ATOM 1758 CZ PHE A 301 92.142 31.157 −12.184 1.00 32.69 A ATOM 1759 C PHE A 301 97.287 34.359 −9.649 1.00 34.23 A ATOM 1760 O PHE A 301 97.784 35.274 −10.303 1.00 33.66 A ATOM 1761 N PRO A 302 97.962 33.750 −8.665 1.00 35.45 A ATOM 1762 CD PRO A 302 97.426 32.932 −27.564 1.00 35.55 A ATOM 1763 CA PRO A 302 99.347 34.145 −8.395 1.00 35.82 A ATOM 1764 CB PRO A 302 99.612 33.571 −7.009 1.00 35.09 A ATOM 1765 CG PRO A 302 98.682 32.401 −6.933 1.00 34.93 A ATOM 1766 C PRO A 302 100.214 33.506 −9.485 1.00 37.48 A ATOM 1767 O PRO A 302 99.830 32.504 −10.083 1.00 37.30 A ATOM 1768 N ALA A 303 101.370 34.100 −9.744 1.00 39.16 A ATOM 1769 CA ALA A 303 102.293 33.641 −10.775 1.00 39.50 A ATOM 1770 CB ALA A 303 103.612 34.393 −10.640 1.00 39.58 A ATOM 1771 C ALA A 303 102.577 32.148 −10.832 1.00 41.05 A ATOM 1772 O ALA A 303 102.642 31.569 −11.920 1.00 42.39 A ATOM 1773 N ALA A 304 102.758 31.526 −9.671 1.00 40.38 A ATOM 1774 CA ALA A 304 103.099 30.105 −9.614 1.00 39.93 A ATOM 1775 CB ALA A 304 103.627 29.772 −8.212 1.00 41.64 A ATOM 1776 C ALA A 304 102.025 29.089 −10.002 1.00 38.27 A ATOM 1777 O ALA A 304 102.343 27.993 −10.453 1.00 39.29 A ATOM 1778 N PHE A 305 100.764 29.453 −9.813 1.00 35.83 A ATOM 1779 CA PHE A 305 99.614 28.587 −10.085 1.00 33.62 A ATOM 1780 CB PHE A 305 98.376 29.475 −10.278 1.00 32.70 A ATOM 1781 CG PHE A 305 97.096 28.857 −9.796 1.00 31.41 A ATOM 1782 CD1 PHE A 305 96.422 27.915 −10.574 1.00 30.30 A ATOM 1783 CD2 PHE A 305 96.556 29.225 −8.562 1.00 30.99 A ATOM 1784 CE1 PHE A 305 95.230 27.350 −10.136 1.00 29.76 A ATOM 1785 CE2 PHE A 305 95.352 28.663 −8.105 1.00 30.08 A ATOM 1786 CZ PHE A 305 94.689 27.725 −8.897 1.00 30.22 A ATOM 1787 C PHE A 305 99.735 27.580 −11.241 1.00 32.03 A ATOM 1788 O PHE A 305 99.767 27.962 −12.405 1.00 32.54 A ATOM 1789 N PHE A 306 99.781 26.290 −10.914 1.00 31.58 A ATOM 1790 CA PHE A 306 99.886 25.235 −11.932 1.00 30.32 A ATOM 1791 CB PHE A 306 99.518 23.875 −11.338 1.00 29.86 A ATOM 1792 CG PHE A 306 100.087 23.639 −9.971 1.00 30.29 A ATOM 1793 CD1 PHE A 306 101.447 23.783 −9.733 1.00 30.37 A ATOM 1794 CD2 PHE A 306 99.259 23.275 −8.919 1.00 30.23 A ATOM 1795 CE1 PHE A 306 101.975 23.570 −8.465 1.00 30.98 A ATOM 1796 CE2 PHE A 306 99.773 23.061 −7.648 1.00 30.91 A ATOM 1797 CZ PHE A 306 101.136 23.210 −7.418 1.00 31.14 A ATOM 1798 C PHE A 306 98.949 25.545 −13.096 1.00 29.48 A ATOM 1799 O PHE A 306 97.738 25.631 −12.920 1.00 30.39 A ATOM 1800 N PRO A 307 99.501 25.701 −14.309 1.00 28.76 A ATOM 1801 CD PRO A 307 100.934 25.575 −14.635 1.00 27.67 A ATOM 1802 CA PRO A 307 98.731 26.014 −15.520 1.00 27.24 A ATOM 1803 CB PRO A 307 99.757 25.848 −16.635 1.00 25.23 A ATOM 1804 CG PRO A 307 101.010 26.262 −15.978 1.00 25.61 A ATOM 1805 C PRO A 307 97.457 25.221 −15.787 1.00 25.86 A ATOM 1806 O PRO A 307 96.419 25.808 −16.098 1.00 24.65 A ATOM 1807 N LYS A 308 97.521 23.901 −15.682 1.00 25.13 A ATOM 1808 CA LYS A 308 96.330 23.109 −15.952 1.00 24.53 A ATOM 1809 CB LYS A 308 96.689 21.640 −16.136 1.00 24.86 A ATOM 1810 CG LYS A 308 97.361 21.413 −17.490 1.00 25.50 A ATOM 1811 CD LYS A 308 97.987 20.047 −17.616 1.00 27.33 A ATOM 1812 CE LYS A 308 98.678 19.886 −18.961 1.00 29.39 A ATOM 1813 NZ LYS A 308 99.232 18.505 −19.146 1.00 32.38 A ATOM 1814 C LYS A 308 95.282 23.293 −14.890 1.00 24.82 A ATOM 1815 O LYS A 308 94.085 23.281 −15.193 1.00 24.89 A ATOM 1816 N ALA A 309 95.716 23.489 −13.647 1.00 24.73 A ATOM 1817 CA ALA A 309 94.758 23.716 −12.573 1.00 25.03 A ATOM 1818 CB ALA A 309 95.445 23.662 −11.208 1.00 24.10 A ATOM 1819 C ALA A 309 94.140 25.094 −12.816 1.00 25.34 A ATOM 1820 O ALA A 309 92.934 25.273 −12.679 1.00 26.34 A ATOM 1821 N ARG A 310 94.958 26.067 −13.198 1.00 26.07 A ATOM 1822 CA ARG A 310 94.419 27.396 −13.453 1.00 28.32 A ATOM 1823 CB ARG A 310 95.513 28.359 −13.908 1.00 29.31 A ATOM 1824 CG ARG A 310 94.940 29.708 −14.288 1.00 31.58 A ATOM 1825 CD ARG A 310 95.917 30.588 −15.030 1.00 31.47 A ATOM 1826 NE ARG A 310 95.275 31.825 −15.473 1.00 34.52 A ATOM 1827 CZ ARG A 310 95.771 33.050 −15.276 1.00 35.51 A ATOM 1828 NH1 ARG A 310 96.929 33.205 −14.633 1.00 33.99 A ATOM 1829 NH2 ARG A 310 95.106 34.124 −15.720 1.00 32.10 A ATOM 1830 C ARG A 310 93.331 27.348 −14.521 1.00 29.03 A ATOM 1831 O ARG A 310 92.308 28.034 −14.418 1.00 29.32 A ATOM 1832 N ASP A 311 93.548 26.536 −15.551 1.00 29.06 A ATOM 1833 CA ASP A 311 92.571 26.432 −16.620 1.00 29.87 A ATOM 1834 CB ASP A 311 93.156 25.636 −17.776 1.00 31.71 A ATOM 1835 CG ASP A 311 92.207 25.537 −18.953 1.00 34.71 A ATOM 1836 OD1 ASP A 311 91.288 24.690 −18.912 1.00 36.90 A ATOM 1837 OD2 ASP A 311 92.378 26.312 −19.918 1.00 36.33 A ATOM 1838 C ASP A 311 91.264 25.800 −16.128 1.00 29.70 A ATOM 1839 O ASP A 311 90.169 26.238 −16.513 1.00 29.95 A ATOM 1840 N LEU A 312 91.383 24.778 −15.282 1.00 26.64 A ATOM 1841 CA LEU A 312 90.215 24.112 −14.715 1.00 24.92 A ATOM 1842 CB LEU A 312 90.645 22.911 −13.869 1.00 23.93 A ATOM 1843 CG LEU A 312 89.504 22.112 −13.227 1.00 24.48 A ATOM 1844 CD1 LEU A 312 88.569 21.610 −14.296 1.00 25.07 A ATOM 1845 CD2 LEU A 312 90.061 20.945 −12.460 1.00 25.13 A ATOM 1846 C LEU A 312 89.412 25.095 −13.841 1.00 23.85 A ATOM 1847 O LEU A 312 88.182 25.136 −13.896 1.00 21.21 A ATOM 1848 N VAL A 313 90.121 25.886 −13.042 1.00 23.12 A ATOM 1849 CA VAL A 313 89.484 26.865 −12.171 1.00 23.55 A ATOM 1850 CB VAL A 313 90.536 27.583 −11.297 1.00 22.33 A ATOM 1851 CG1 VAL A 313 89.898 28.752 −10.559 1.00 19.05 A ATOM 1852 CG2 VAL A 313 91.144 26.607 −10.305 1.00 19.89 A ATOM 1853 C VAL A 313 88.701 27.915 −12.975 1.00 25.59 A ATOM 1854 O VAL A 313 87.590 28.305 −12.605 1.00 26.57 A ATOM 1855 N GLU A 314 89.278 28.378 −14.076 1.00 26.08 A ATOM 1856 CA GLU A 314 88.598 29.370 −14.895 1.00 26.79 A ATOM 1857 CB GLU A 314 89.543 29.928 −15.948 1.00 27.50 A ATOM 1858 CG GLU A 314 90.739 30.639 −15.381 1.00 32.29 A ATOM 1859 CD GLU A 314 91.687 31.094 −16.463 1.00 35.85 A ATOM 1860 OE1 GLU A 314 91.967 30.280 −17.375 1.00 38.06 A ATOM 1861 OE2 GLU A 314 92.157 32.257 −16.399 1.00 38.48 A ATOM 1862 C GLU A 314 87.370 28.787 −15.577 1.00 26.22 A ATOM 1863 O GLU A 314 86.499 29.527 −16.038 1.00 27.23 A ATOM 1864 N LYS A 315 87.300 27.464 −15.662 1.00 24.74 A ATOM 1865 CA LYS A 315 86.151 26.832 −16.294 1.00 23.60 A ATOM 1866 CB LYS A 315 86.578 25.584 −17.073 1.00 23.69 A ATOM 1867 CG LYS A 315 87.393 25.865 −18.344 1.00 22.41 A ATOM 1868 CD LYS A 315 87.825 24.545 −18.968 1.00 25.68 A ATOM 1869 CE LYS A 315 88.768 24.695 −20.155 1.00 24.86 A ATOM 1870 NZ LYS A 315 88.082 25.219 −21.346 1.00 28.62 A ATOM 1871 C LYS A 315 85.119 26.471 −15.230 1.00 23.42 A ATOM 1872 O LYS A 315 84.043 25.970 −15.541 1.00 25.37 A ATOM 1873 N LEU A 316 85.454 26.730 −13.970 1.00 21.88 A ATOM 1874 CA LEU A 316 84.549 26.461 −12.862 1.00 20.21 A ATOM 1875 CB LEU A 316 85.272 25.705 −11.767 1.00 19.57 A ATOM 1876 CG LEU A 316 85.409 24.221 −12.078 1.00 21.14 A ATOM 1877 CD1 LEU A 316 86.272 23.552 −11.009 1.00 19.21 A ATOM 1878 CD2 LEU A 316 84.000 23.600 −12.166 1.00 18.59 A ATOM 1879 C LEU A 316 83.996 27.758 −12.290 1.00 21.31 A ATOM 1880 O LEU A 316 82.811 27.848 −11.955 1.00 18.79 A ATOM 1881 N LEU A 317 84.865 28.762 −12.175 1.00 20.59 A ATOM 1882 CA LEU A 317 84.446 30.038 −11.646 1.00 21.64 A ATOM 1883 CB LEU A 317 85.606 30.707 −10.900 1.00 21.42 A ATOM 1884 CG LEU A 317 86.130 29.892 −9.711 1.00 21.80 A ATOM 1885 CD1 LEU A 317 87.299 30.599 −9.047 1.00 23.09 A ATOM 1886 CD2 LEU A 317 85.031 29.688 −8.724 1.00 20.34 A ATOM 1887 C LEU A 317 83.940 30.890 −12.810 1.00 23.34 A ATOM 1888 O LEU A 317 84.568 31.859 −13.242 1.00 23.29 A ATOM 1889 N VAL A 318 82.786 30.485 −13.324 1.00 24.06 A ATOM 1890 CA VAL A 318 82.135 31.161 −14.436 1.00 23.46 A ATOM 1891 CB VAL A 318 81.829 30.150 −15.547 1.00 24.32 A ATOM 1892 CG1 VAL A 318 81.061 30.828 −16.670 1.00 22.57 A ATOM 1893 CG2 VAL A 318 83.136 29.524 −16.049 1.00 20.68 A ATOM 1894 C VAL A 318 80.838 31.765 −13.918 1.00 24.59 A ATOM 1895 O VAL A 318 80.050 31.086 −13.250 1.00 24.86 A ATOM 1896 N LEU A 319 80.603 33.036 −14.215 1.00 24.95 A ATOM 1897 CA LEU A 319 79.383 33.688 −13.731 1.00 25.79 A ATOM 1898 CB LEU A 319 79.379 35.157 −14.154 1.00 25.38 A ATOM 1899 CG LEU A 319 80.466 35.963 −13.417 1.00 27.04 A ATOM 1900 CD1 LEU A 319 80.452 37.421 −13.869 1.00 25.54 A ATOM 1901 CD2 LEU A 319 80.241 35.872 −11.907 1.00 23.27 A ATOM 1902 C LEU A 319 78.077 32.989 −14.141 1.00 26.05 A ATOM 1903 O LEU A 319 77.171 32.819 −13.319 1.00 27.69 A ATOM 1904 N ASP A 320 77.982 32.580 −15.400 1.00 25.08 A ATOM 1905 CA ASP A 320 76.804 31.881 −15.892 1.00 24.00 A ATOM 1906 CB ASP A 320 76.788 31.907 −17.420 1.00 24.02 A ATOM 1907 CG ASP A 320 75.597 31.175 −17.996 1.00 27.27 A ATOM 1908 OD1 ASP A 320 75.009 30.337 −17.271 1.00 29.66 A ATOM 1909 OD2 ASP A 320 75.253 31.417 −19.175 1.00 30.03 A ATOM 1910 C ASP A 320 76.846 30.427 −15.396 1.00 24.04 A ATOM 1911 O ASP A 320 77.661 29.623 −15.846 1.00 25.11 A ATOM 1912 N ALA A 321 75.940 30.094 −14.489 1.00 23.73 A ATOM 1913 CA ALA A 321 75.867 28.770 −13.887 1.00 23.58 A ATOM 1914 CB ALA A 321 74.710 28.720 −12.916 1.00 23.62 A ATOM 1915 C ALA A 321 75.765 27.599 −14.853 1.00 24.90 A ATOM 1916 O ALA A 321 76.221 26.497 −14.549 1.00 24.36 A ATOM 1917 N THR A 322 75.176 27.834 −16.019 1.00 25.50 A ATOM 1918 CA THR A 322 75.008 26.772 −17.011 1.00 24.60 A ATOM 1919 CB THR A 322 73.816 27.064 −17.909 1.00 23.09 A ATOM 1920 OG1 THR A 322 74.079 28.263 −18.646 1.00 23.74 A ATOM 1921 CG2 THR A 322 72.568 27.260 −17.080 1.00 20.71 A ATOM 1922 C THR A 322 76.238 26.596 −17.893 1.00 25.24 A ATOM 1923 O THR A 322 76.221 25.807 −18.832 1.00 26.45 A ATOM 1924 N LYS A 323 77.300 27.331 −17.592 1.00 25.05 A ATOM 1925 CA LYS A 323 78.526 27.239 −18.366 1.00 26.46 A ATOM 1926 CB LYS A 323 78.972 28.627 −18.823 1.00 28.68 A ATOM 1927 CG LYS A 323 78.050 29.304 −19.814 1.00 31.27 A ATOM 1928 CD LYS A 323 78.470 29.004 −21.240 1.00 34.38 A ATOM 1929 CE LYS A 323 77.850 29.986 −22.243 1.00 35.12 A ATOM 1930 NZ LYS A 323 76.363 29.936 −22.251 1.00 36.71 A ATOM 1931 C LYS A 323 79.660 26.621 −17.556 1.00 26.39 A ATOM 1932 O LYS A 323 80.795 26.615 −18.010 1.00 28.51 A ATOM 1933 N ARG A 324 79.372 26.114 −16.360 1.00 24.50 A ATOM 1934 CA ARG A 324 80.429 25.524 −15.543 1.00 23.37 A ATOM 1935 CB ARG A 324 80.087 25.633 −14.049 1.00 23.41 A ATOM 1936 CG ARG A 324 80.233 27.034 −13.520 1.00 21.60 A ATOM 1937 CD ARG A 324 79.594 27.220 −12.173 1.00 21.55 A ATOM 1938 NE ARG A 324 79.245 28.624 −11.986 1.00 19.69 A ATOM 1939 CZ ARG A 324 78.273 29.054 −11.191 1.00 19.84 A ATOM 1940 NH1 ARG A 324 77.555 28.183 −10.496 1.00 16.83 A ATOM 1941 NH2 ARG A 324 77.990 30.358 −11.129 1.00 21.41 A ATOM 1942 C ARG A 324 80.717 24.085 −15.897 1.00 22.63 A ATOM 1943 O ARG A 324 79.798 23.280 −16.058 1.00 24.44 A ATOM 1944 N LEU A 325 82.000 23.767 −16.023 1.00 20.68 A ATOM 1945 CA LEU A 325 82.414 22.411 −16.352 1.00 20.98 A ATOM 1946 CB LEU A 325 83.952 22.330 −16.386 1.00 20.82 A ATOM 1947 CG LEU A 325 84.596 21.147 −17.131 1.00 23.08 A ATOM 1948 CD1 LEU A 325 84.149 21.194 −18.595 1.00 21.39 A ATOM 1949 CD2 LEU A 325 86.132 21.173 −17.038 1.00 20.00 A ATOM 1950 C LEU A 325 81.840 21.454 −15.290 1.00 20.43 A ATOM 1951 O LEU A 325 82.062 21.633 −14.097 1.00 18.45 A ATOM 1952 N GLY A 326 81.076 20.456 −15.725 1.00 21.33 A ATOM 1953 CA GLY A 326 80.501 19.513 −14.778 1.00 20.60 A ATOM 1954 C GLY A 326 78.984 19.523 −14.701 1.00 22.39 A ATOM 1955 O GLY A 326 78.383 18.493 −14.378 1.00 22.59 A ATOM 1956 N CYS A 327 78.358 20.664 −15.009 1.00 23.36 A ATOM 1957 CA CYS A 327 76.896 20.771 −14.963 1.00 25.18 A ATOM 1958 CB CYS A 327 76.453 22.246 −14.889 1.00 25.79 A ATOM 1959 SG CYS A 327 76.742 23.237 −16.364 1.00 31.42 A ATOM 1960 C CYS A 327 76.229 20.074 −16.148 1.00 24.99 A ATOM 1961 O CYS A 327 76.887 19.743 −17.129 1.00 24.31 A ATOM 1962 N ALA A 328 74.923 19.847 −16.040 1.00 26.34 A ATOM 1963 CA ALA A 328 74.157 19.172 −17.094 1.00 27.51 A ATOM 1964 CB ALA A 328 72.703 18.949 −16.629 1.00 26.81 A ATOM 1965 C ALA A 328 74.179 19.905 −18.443 1.00 28.11 A ATOM 1966 O ALA A 328 74.243 19.274 −19.501 1.00 27.66 A ATOM 1967 N GLU A 329 74.144 21.231 −18.418 1.00 28.05 A ATOM 1968 CA GLU A 329 74.172 21.973 −19.668 1.00 29.54 A ATOM 1969 CB GLU A 329 73.915 23.458 −19.428 1.00 32.18 A ATOM 1970 CG GLU A 329 72.539 23.783 −18.863 1.00 37.89 A ATOM 1971 CD GLU A 329 72.418 23.503 −17.374 1.00 41.37 A ATOM 1972 OE1 GLU A 329 73.464 23.308 −16.711 1.00 43.80 A ATOM 1973 OE2 GLU A 329 71.273 23.495 −16.863 1.00 43.66 A ATOM 1974 C GLU A 329 75.514 21.807 −20.377 1.00 29.08 A ATOM 1975 O GLU A 329 75.602 21.927 −21.605 1.00 27.73 A ATOM 1976 N MET A 330 76.559 21.540 −19.598 1.00 27.54 A ATOM 1977 CA MET A 330 77.894 21.359 −20.148 1.00 25.71 A ATOM 1978 CB MET A 330 78.945 21.963 −19.219 1.00 27.88 A ATOM 1979 CG MET A 330 78.964 23.489 −19.209 1.00 30.29 A ATOM 1980 SD MET A 330 79.429 24.194 −20.819 1.00 34.04 A ATOM 1981 CE MET A 330 81.187 23.670 −20.936 1.00 29.55 A ATOM 1982 C MET A 330 78.156 19.884 −20.343 1.00 24.53 A ATOM 1983 O MET A 330 79.290 19.473 −20.575 1.00 22.65 A ATOM 1984 N GLU A 331 77.089 19.095 −20.221 1.00 22.87 A ATOM 1985 CA GLU A 331 77.139 17.654 −20.415 1.00 21.38 A ATOM 1986 CB GLU A 331 77.854 17.339 −21.735 1.00 22.71 A ATOM 1987 CG GLU A 331 76.903 16.916 −22.837 1.00 23.01 A ATOM 1988 CD GLU A 331 75.599 17.720 −22.875 1.00 24.76 A ATOM 1989 OE1 GLU A 331 75.570 18.830 −23.441 1.00 26.12 A ATOM 1990 OE2 GLU A 331 74.588 17.230 −22.337 1.00 24.22 A ATOM 1991 C GLU A 331 77.671 16.765 −19.290 1.00 21.01 A ATOM 1992 O GLU A 331 78.075 15.619 −19.517 1.00 19.50 A ATOM 1993 N GLY A 332 77.675 17.284 −18.071 1.00 19.73 A ATOM 1994 CA GLY A 332 78.056 16.445 −16.954 1.00 17.80 A ATOM 1995 C GLY A 332 79.494 16.243 −16.570 1.00 17.28 A ATOM 1996 O GLY A 332 80.381 17.013 −16.934 1.00 16.11 A ATOM 1997 N TYR A 333 79.701 15.151 −15.842 1.00 16.52 A ATOM 1998 CA TYR A 333 80.997 14.791 −15.305 1.00 16.75 A ATOM 1999 CB TYR A 333 80.787 13.854 −14.115 1.00 16.95 A ATOM 2000 CG TYR A 333 80.369 14.624 −12.893 1.00 18.08 A ATOM 2001 CD1 TYR A 333 81.332 15.207 −12.059 1.00 18.77 A ATOM 2002 CE1 TYR A 333 80.971 16.035 −10.982 1.00 17.69 A ATOM 2003 CD2 TYR A 333 79.021 14.877 −12.620 1.00 17.08 A ATOM 2004 CE2 TYR A 333 78.646 15.713 −11.538 1.00 19.05 A ATOM 2005 CZ TYR A 333 79.640 16.287 −10.728 1.00 18.04 A ATOM 2006 OH TYR A 333 79.322 17.126 −9.682 1.00 18.69 A ATOM 2007 C TYR A 333 82.051 14.240 −16.238 1.00 16.78 A ATOM 2008 O TYR A 333 83.248 14.393 −15.977 1.00 16.04 A ATOM 2009 N GLY A 334 81.633 13.598 −17.321 1.00 16.63 A ATOM 2010 CA GLY A 334 82.624 13.082 −18.244 1.00 17.02 A ATOM 2011 C GLY A 334 83.576 14.194 −18.683 1.00 17.47 A ATOM 2012 O GLY A 334 84.802 14.063 −18.562 1.00 17.18 A ATOM 2013 N PRO A 335 83.039 15.315 −19.195 1.00 17.04 A ATOM 2014 CD PRO A 335 81.650 15.611 −19.590 1.00 16.18 A ATOM 2015 CA PRO A 335 83.940 16.382 −19.621 1.00 17.35 A ATOM 2016 CB PRO A 335 82.991 17.441 −20.178 1.00 17.48 A ATOM 2017 CG PRO A 335 81.857 16.605 −20.713 1.00 18.64 A ATOM 2018 C PRO A 335 84.786 16.883 −18.480 1.00 18.48 A ATOM 2019 O PRO A 335 85.963 17.131 −18.661 1.00 20.84 A ATOM 2020 N LEU A 336 84.204 17.034 −17.299 1.00 19.46 A ATOM 2021 CA LEU A 336 84.986 17.504 −16.153 1.00 19.38 A ATOM 2022 CB LEU A 336 84.071 17.692 −14.937 1.00 18.98 A ATOM 2023 CG LEU A 336 84.765 17.982 −13.604 1.00 18.01 A ATOM 2024 CD1 LEU A 336 85.534 19.289 −13.690 1.00 16.66 A ATOM 2025 CD2 LEU A 336 83.724 18.055 −12.491 1.00 18.81 A ATOM 2026 C LEU A 336 86.132 16.528 −15.815 1.00 19.32 A ATOM 2027 O LEU A 336 87.293 16.932 −15.683 1.00 18.65 A ATOM 2028 N LYS A 337 85.808 15.244 −15.688 1.00 18.38 A ATOM 2029 CA LYS A 337 86.821 14.240 −15.387 1.00 18.89 A ATOM 2030 CB LYS A 337 86.147 12.900 −15.082 1.00 17.70 A ATOM 2031 CG LYS A 337 85.460 12.933 −13.727 1.00 19.89 A ATOM 2032 CD LYS A 337 84.450 11.817 −13.523 1.00 22.66 A ATOM 2033 CE LYS A 337 85.089 10.453 −13.372 1.00 22.78 A ATOM 2034 NZ LYS A 337 84.025 9.444 −13.088 1.00 25.28 A ATOM 2035 C LYS A 337 87.865 14.101 −16.504 1.00 20.07 A ATOM 2036 O LYS A 337 88.996 13.671 −16.254 1.00 20.47 A ATOM 2037 N ALA A 338 87.491 14.486 −17.725 1.00 20.38 A ATOM 2038 CA ALA A 338 88.393 14.441 −18.876 1.00 20.65 A ATOM 2039 CB ALA A 338 87.580 14.382 −20.178 1.00 20.29 A ATOM 2040 C ALA A 338 89.357 15.636 −18.933 1.00 22.18 A ATOM 2041 O ALA A 338 90.265 15.665 −19.768 1.00 24.71 A ATOM 2042 N HIS A 339 89.179 16.627 −18.063 1.00 21.90 A ATOM 2043 CA HIS A 339 90.072 17.785 −18.094 1.00 22.10 A ATOM 2044 CB HIS A 339 89.711 18.762 −16.989 1.00 21.35 A ATOM 2045 CG HIS A 339 90.357 20.097 −17.149 1.00 20.57 A ATOM 2046 CD2 HIS A 339 89.891 21.251 −17.683 1.00 19.19 A ATOM 2047 ND1 HIS A 339 91.664 20.341 −16.783 1.00 20.52 A ATOM 2048 CE1 HIS A 339 91.973 21.592 −17.085 1.00 22.28 A ATOM 2049 NE2 HIS A 339 90.914 22.165 −17.633 1.00 21.96 A ATOM 2050 C HIS A 339 91.555 17.404 −17.963 1.00 22.78 A ATOM 2051 O HIS A 339 91.919 16.600 −17.118 1.00 21.05 A ATOM 2052 N PRO A 340 92.425 17.994 −18.801 1.00 24.12 A ATOM 2053 CD PRO A 340 92.090 18.973 −19.855 1.00 23.53 A ATOM 2054 CA PRO A 340 93.872 17.724 −18.795 1.00 25.11 A ATOM 2055 CB PRO A 340 94.435 18.864 −19.647 1.00 22.31 A ATOM 2056 CG PRO A 340 93.379 19.015 −20.685 1.00 22.50 A ATOM 2057 C PRO A 340 94.540 17.654 −17.421 1.00 25.66 A ATOM 2058 O PRO A 340 95.523 16.951 −17.237 1.00 27.43 A ATOM 2059 N PHE A 341 94.011 18.389 −16.459 1.00 25.05 A ATOM 2060 CA PHE A 341 94.596 18.399 −15.139 1.00 24.88 A ATOM 2061 CB PHE A 341 93.897 19.459 −14.276 1.00 24.71 A ATOM 2062 CG PHE A 341 94.482 19.607 −12.893 1.00 24.42 A ATOM 2063 CD1 PHE A 341 95.822 19.947 −12.721 1.00 22.55 A ATOM 2064 CD2 PHE A 341 93.685 19.397 −11.758 1.00 22.61 A ATOM 2065 CE1 PHE A 341 96.364 20.076 −11.434 1.00 23.65 A ATOM 2066 CE2 PHE A 341 94.204 19.522 −10.476 1.00 22.09 A ATOM 2067 CZ PHE A 341 95.547 19.863 −10.304 1.00 24.01 A ATOM 2068 C PHE A 341 94.511 17.026 −14.486 1.00 25.70 A ATOM 2069 O PHE A 341 95.363 16.665 −13.680 1.00 27.11 A ATOM 2070 N PHE A 342 93.499 16.258 −14.865 1.00 25.51 A ATOM 2071 CA PHE A 342 93.262 14.929 −14.318 1.00 25.34 A ATOM 2072 CB PHE A 342 91.758 14.728 −14.120 1.00 21.93 A ATOM 2073 CG PHE A 342 91.120 15.728 −13.196 1.00 20.26 A ATOM 2074 CD1 PHE A 342 91.556 15.862 −11.888 1.00 20.03 A ATOM 2075 CD2 PHE A 342 90.030 16.485 −13.613 1.00 19.36 A ATOM 2076 CE1 PHE A 342 90.907 16.731 −11.004 1.00 19.87 A ATOM 2077 CE2 PHE A 342 89.377 17.348 −12.744 1.00 18.17 A ATOM 2078 CZ PHE A 342 89.818 17.470 −11.431 1.00 19.27 A ATOM 2079 C PHE A 342 93.805 13.815 −15.214 1.00 27.64 A ATOM 2080 O PHE A 342 93.508 12.630 −15.019 1.00 27.39 A ATOM 2081 N GLU A 343 94.607 14.203 −16.194 1.00 31.32 A ATOM 2082 CA GLU A 343 95.185 13.262 −17.150 1.00 34.29 A ATOM 2083 CB GLU A 343 96.320 13.950 −17.889 1.00 38.36 A ATOM 2084 CG GLU A 343 96.735 13.314 −19.197 1.00 45.23 A ATOM 2085 CD GLU A 343 97.654 14.247 −19.976 1.00 51.01 A ATOM 2086 OE1 GLU A 343 98.266 13.801 −20.981 1.00 51.76 A ATOM 2087 OE2 GLU A 343 97.755 15.439 −19.568 1.00 52.42 A ATOM 2088 C GLU A 343 95.690 11.950 −16.542 1.00 33.50 A ATOM 2089 O GLU A 343 95.289 10.860 −16.970 1.00 33.57 A ATOM 2090 N SER A 344 96.554 12.049 −15.537 1.00 31.58 A ATOM 2091 CA SER A 344 97.117 10.857 −14.906 1.00 30.38 A ATOM 2092 CB SER A 344 98.447 11.217 −14.253 1.00 29.76 A ATOM 2093 OG SER A 344 98.243 11.995 −13.096 1.00 30.32 A ATOM 2094 C SER A 344 96.242 10.150 −13.857 1.00 30.00 A ATOM 2095 O SER A 344 96.662 9.137 −13.285 1.00 31.14 A ATOM 2096 N VAL A 345 95.046 10.679 −13.606 1.00 27.28 A ATOM 2097 CA VAL A 345 94.135 10.126 −12.609 1.00 25.39 A ATOM 2098 CB VAL A 345 93.093 11.213 −12.159 1.00 24.17 A ATOM 2099 CG1 VAL A 345 91.973 10.568 −11.347 1.00 19.50 A ATOM 2100 CG2 VAL A 345 93.779 12.321 −11.363 1.00 17.85 A ATOM 2101 C VAL A 345 93.341 8.885 −13.043 1.00 26.45 A ATOM 2102 O VAL A 345 92.813 8.842 −14.154 1.00 27.42 A ATOM 2103 N THR A 346 93.253 7.890 −12.157 1.00 26.62 A ATOM 2104 CA THR A 346 92.451 6.680 −12.406 1.00 27.91 A ATOM 2105 CB THR A 346 93.194 5.388 −11.999 1.00 29.18 A ATOM 2106 OG1 THR A 346 94.345 5.224 −12.830 1.00 33.51 A ATOM 2107 CG2 THR A 346 92.300 4.171 −12.177 1.00 28.24 A ATOM 2108 C THR A 346 91.229 6.856 −11.505 1.00 27.53 A ATOM 2109 O THR A 346 91.297 6.621 −10.299 1.00 29.24 A ATOM 2110 N TRP A 347 90.117 7.279 −12.094 1.00 27.83 A ATOM 2111 CA TRP A 347 88.898 7.561 −11.336 1.00 29.15 A ATOM 2112 CB TRP A 347 87.878 8.278 −12.224 1.00 27.12 A ATOM 2113 CG TRP A 347 88.353 9.574 −12.758 1.00 25.48 A ATOM 2114 CD2 TRP A 347 88.252 10.853 −12.118 1.00 24.27 A ATOM 2115 CE2 TRP A 347 88.841 11.803 −12.990 1.00 23.82 A ATOM 2116 CE3 TRP A 347 87.723 11.292 −10.897 1.00 22.42 A ATOM 2117 CD1 TRP A 347 88.984 9.788 −13.952 1.00 24.47 A ATOM 2118 NE1 TRP A 347 89.279 11.124 −14.099 1.00 23.92 A ATOM 2119 CZ2 TRP A 347 88.913 13.169 −12.678 1.00 21.68 A ATOM 2120 CZ3 TRP A 347 87.797 12.654 −10.586 1.00 24.15 A ATOM 2121 CH2 TRP A 347 88.391 13.575 −11.480 1.00 22.35 A ATOM 2122 C TRP A 347 88.218 6.370 −10.700 1.00 30.64 A ATOM 2123 O TRP A 347 87.617 6.476 −9.631 1.00 31.21 A ATOM 2124 N GLU A 348 88.318 5.242 −11.376 1.00 32.16 A ATOM 2125 CA GLU A 348 87.698 4.003 −10.952 1.00 34.98 A ATOM 2126 CB GLU A 348 88.157 2.890 −11.904 1.00 37.47 A ATOM 2127 CG GLU A 348 87.815 3.125 −13.419 1.00 41.39 A ATOM 2128 CD GLU A 348 88.619 4.257 −14.116 1.00 41.83 A ATOM 2129 OE1 GLU A 348 89.828 4.408 −13.841 1.00 42.27 A ATOM 2130 OE2 GLU A 348 88.036 4.982 −14.959 1.00 42.41 A ATOM 2131 C GLU A 348 87.843 3.547 −9.478 1.00 34.74 A ATOM 2132 O GLU A 348 86.866 3.111 −8.869 1.00 35.95 A ATOM 2133 N ASN A 349 89.024 3.652 −8.887 1.00 33.61 A ATOM 2134 CA ASN A 349 89.189 3.179 −7.507 1.00 32.34 A ATOM 2135 CB ASN A 349 89.936 1.860 −7.529 1.00 33.21 A ATOM 2136 CG ASN A 349 91.345 2.016 −8.089 1.00 34.48 A ATOM 2137 OD1 ASN A 349 91.613 2.943 −8.858 1.00 32.91 A ATOM 2138 ND2 ASN A 349 92.247 1.110 −7.712 1.00 35.85 A ATOM 2139 C ASN A 349 89.949 4.136 −6.594 1.00 31.22 A ATOM 2140 O ASN A 349 90.826 3.714 −5.839 1.00 31.07 A ATOM 2141 N LEU A 350 89.611 5.416 −6.646 1.00 28.54 A ATOM 2142 CA LEU A 350 90.300 6.403 −5.837 1.00 26.75 A ATOM 2143 CB LEU A 350 89.632 7.762 −6.024 1.00 25.89 A ATOM 2144 CG LEU A 350 90.095 8.558 −7.239 1.00 24.21 A ATOM 2145 CD1 LEU A 350 89.111 9.674 −7.547 1.00 23.55 A ATOM 2146 CD2 LEU A 350 91.475 9.118 −6.932 1.00 23.67 A ATOM 2147 C LEU A 350 90.440 6.102 −4.345 1.00 27.67 A ATOM 2148 O LEU A 350 91.478 6.401 −3.753 1.00 28.06 A ATOM 2149 N HIS A 351 89.424 5.509 −3.722 1.00 27.81 A ATOM 2150 CA HIS A 351 89.539 5.254 −2.299 1.00 29.88 A ATOM 2151 CB HIS A 351 88.144 5.197 −1.646 1.00 31.47 A ATOM 2152 CG HIS A 351 87.584 3.823 −1.475 1.00 32.65 A ATOM 2153 CD2 HIS A 351 86.926 3.009 −2.338 1.00 34.75 A ATOM 2154 ND1 HIS A 351 87.629 3.150 −0.273 1.00 34.31 A ATOM 2155 CE1 lHIS A 351 87.022 1.981 −0.402 1.00 36.41 A ATOM 2156 NE2 HIS A 351 86.586 1.871 −1.644 1.00 35.36 A ATOM 2157 C HIS A 351 90.396 4.030 −1.978 1.00 30.93 A ATOM 2158 O HIS A 351 90.674 3.741 −0.812 1.00 31.57 A ATOM 2159 N GLN A 352 90.842 3.337 −3.022 1.00 31.09 A ATOM 2160 CA GLN A 352 91.709 2.177 −2.864 1.00 31.86 A ATOM 2161 CB GLN A 352 91.482 1.187 −3.992 1.00 35.63 A ATOM 2162 CG GLN A 352 91.038 0.141 −3.497 1.00 40.62 A ATOM 2163 CD GLN A 352 89.739 0.036 −2.766 1.00 42.39 A ATOM 2164 OE1 GLN A 352 88.684 0.133 −3.376 1.00 44.19 A ATOM 2165 NE2 GLN A 352 89.802 0.112 −1.447 1.00 44.81 A ATOM 2166 C GLN A 352 93.167 2.626 −2.907 1.00 31.39 A ATOM 2167 O GLN A 352 94.030 2.022 −2.271 1.00 31.44 A ATOM 2168 N GLN A 353 93.429 3.685 −3.672 1.00 29.13 A ATOM 2169 CA GLN A 353 94.769 4.237 −3.813 1.00 27.37 A ATOM 2170 CB GLN A 353 94.767 5.283 −4.932 1.00 25.81 A ATOM 2171 CG GLN A 353 94.250 4.702 −6.242 1.00 26.68 A ATOM 2172 CD GLN A 353 94.035 5.738 −7.330 1.00 26.81 A ATOM 2173 OE1 GLN A 353 94.792 6.709 −7.435 1.00 25.21 A ATOM 2174 NE2 GLN A 353 93.011 5.520 −8.171 1.00 24.24 A ATOM 2175 C GLN A 353 95.288 4.851 −2.510 1.00 28.25 A ATOM 2176 O GLN A 353 94.511 5.245 −1.633 1.00 28.38 A ATOM 2177 N THR A 354 96.608 4.907 −2.375 1.00 28.16 A ATOM 2178 CA THR A 354 97.220 5.489 −1.193 1.00 28.54 A ATOM 2179 CB THR A 354 98.564 4.848 −0.889 1.00 29.50 A ATOM 2180 OG1 THR A 354 98.354 3.459 −0.624 1.00 31.62 A ATOM 2181 CG2 THR A 354 99.225 5.517 0.334 1.00 27.68 A ATOM 2182 C THR A 354 97.438 6.955 −1.468 1.00 27.76 A ATOM 2183 O THR A 354 98.062 7.307 −2.453 1.00 27.12 A ATOM 2184 N PRO A 355 96.928 7.832 −0.592 1.00 28.37 A ATOM 2185 CD PRO A 355 96.067 7.582 0.573 1.00 27.67 A ATOM 2186 CA PRO A 355 97.092 9.266 −0.802 1.00 28.53 A ATOM 2187 CB PRO A 355 96.215 9.883 0.291 1.00 28.29 A ATOM 2188 CG PRO A 355 95.210 8.807 0.579 1.00 28.38 A ATOM 2189 C PRO A 355 98.528 9.724 −0.695 1.00 28.85 A ATOM 2190 O PRO A 355 99.290 9.232 0.139 1.00 29.42 A ATOM 2191 N PRO A 356 98.916 10.676 −1.548 1.00 28.20 A ATOM 2192 CD PRO A 356 98.083 11.340 −2.567 1.00 27.35 A ATOM 2193 CA PRO A 356 100.276 11.213 −1.539 1.00 28.63 A ATOM 2194 CB PRO A 356 100.261 12.199 −2.712 1.00 29.02 A ATOM 2195 CG PRO A 356 98.815 12.633 −2.781 1.00 27.44 A ATOM 2196 C PRO A 356 100.483 11.899 −0.195 1.00 29.18 A ATOM 2197 O PRO A 356 99.543 12.505 0.331 1.00 28.80 A ATOM 2198 N ALA A 357 101.689 11.806 0.368 1.00 29.69 A ATOM 2199 CA ALA A 357 101.942 12.439 1.664 1.00 31.97 A ATOM 2200 CB ALA A 357 103.273 11.964 2.253 1.00 29.11 A ATOM 2201 C ALA A 357 101.928 13.964 1.528 1.00 33.61 A ATOM 2202 O ALA A 357 102.371 14.507 0.520 1.00 33.81 A ATOM 2203 N LEU A 358 101.390 14.645 2.540 1.00 36.37 A ATOM 2204 CA LEU A 358 101.295 16.110 2.543 1.00 38.03 A ATOM 2205 CB LEU A 358 99.995 16.554 3.209 1.00 36.49 A ATOM 2206 CG LEU A 358 98.679 16.059 2.641 1.00 35.57 A ATOM 2207 CD1 LEU A 358 97.568 16.398 3.620 1.00 35.78 A ATOM 2208 CD2 LEU A 358 98.443 16.689 1.278 1.00 37.10 A ATOM 2209 C LEU A 358 102.460 16.743 3.310 1.00 39.05 A ATOM 2210 O LEU A 358 102.451 16.592 4.553 1.00 39.24 A ATOM 2211 OXT LEU A 358 103.348 17.370 2.679 1.00 40.12 A ATOM 2212 OH2 TIP S 1 82.347 32.462 −3.850 1.00 16.08 S ATOM 2213 OH2 TIP S 4 80.761 19.051 −18.244 1.00 23.37 S ATOM 2214 OH2 TIP S 7 79.269 13.051 −18.353 1.00 22.32 S ATOM 2215 OH2 TIP S 8 86.710 32.919 −1.646 1.00 24.05 S ATOM 2216 OH2 TIP S 9 78.564 −0.823 16.465 1.00 28.00 S ATOM 2217 OH2 TIP S 10 75.323 16.274 8.538 1.00 18.43 S ATOM 2218 OH2 TIP S 12 78.540 24.328 −2.128 1.00 27.08 S ATOM 2219 OH2 TIP S 13 91.533 13.928 −17.231 1.00 22.56 S ATOM 2220 OH2 TIP S 14 77.419 −0.445 24.044 1.00 23.98 S ATOM 2221 OH2 TIP S 19 72.498 40.164 −3.114 1.00 21.78 S ATOM 2222 OH2 TIP S 20 77.303 13.198 −15.393 1.00 22.49 S ATOM 2223 OH2 TIP S 21 75.600 −1.063 22.040 1.00 24.29 S ATOM 2224 OH2 TIP S 22 90.133 19.697 12.606 1.00 16.61 S ATOM 2225 OH2 TIP S 24 74.810 7.002 25.700 1.00 20.66 S ATOM 2226 OH2 TIP S 27 74.894 8.778 −8.074 1.00 23.31 S ATOM 2227 OH2 TIP S 28 80.070 33.741 −17.170 1.00 27.29 S ATOM 2228 OH2 TIP S 31 74.744 21.007 3.348 1.00 29.98 S ATOM 2229 OH2 TIP S 32 97.930 12.301 2.472 1.00 16.75 S ATOM 2230 OH2 TIP S 35 78.412 7.338 3.002 1.00 16.51 S ATOM 2231 OH2 TIP S 36 80.172 27.171 1.300 1.00 34.66 S ATOM 2232 OH2 TIP S 41 69.773 3.412 17.444 1.00 24.08 S ATOM 2233 OH2 TIP S 43 88.878 7.904 10.616 1.00 20.34 S ATOM 2234 OH2 TIP S 44 87.375 32.487 −13.928 1.00 31.99 S ATOM 2235 OH2 TIP S 45 91.671 10.803 −16.123 1.00 35.59 S ATOM 2236 OH2 TIP S 46 87.637 11.564 23.703 1.00 22.67 S ATOM 2237 OH2 TIP S 48 93.353 28.739 3.547 1.00 32.79 S ATOM 2238 OH2 TIP S 50 82.283 34.597 −16.032 1.00 23.90 S ATOM 2239 OH2 TIP S 52 81.673 8.965 −8.348 1.00 27.83 S ATOM 2240 OH2 TIP S 55 94.012 3.488 1.399 1.00 24.78 S ATOM 2241 OH2 TIP S 58 85.735 11.257 −18.436 1.00 27.15 S ATOM 2242 OH2 TIP S 61 79.069 −4.638 12.345 1.00 21.04 S ATOM 2243 OH2 TIP S 64 103.981 17.563 −7.228 1.00 28.86 S ATOM 2244 OH2 TIP S 66 79.020 43.119 5.431 1.00 33.30 S ATOM 2245 OH2 TIP S 69 88.177 36.956 3.079 1.00 30.87 S ATOM 2246 OH2 TIP S 75 78.707 27.486 −3.439 1.00 25.25 S ATOM 2247 OH2 TIP S 79 80.347 33.345 6.422 1.00 38.57 S ATOM 2248 OH2 TIP S 84 64.594 19.493 24.406 1.00 26.01 S ATOM 2249 OH2 TIP S 98 70.215 21.980 19.413 1.00 24.75 S ATOM 2250 OH2 TIP S 116 103.456 14.637 −2.925 1.00 41.84 S ATOM 2251 OH2 TIP S 120 97.528 14.189 −14.706 1.00 43.27 S ATOM 2252 OH2 TIP S 128 103.602 10.418 −1.388 1.00 37.07 S ATOM 2253 OH2 TIP S 129 83.353 33.273 4.410 1.00 34.78 S ATOM 2254 OH2 TIP S 130 74.116 4.597 −3.022 1.00 27.69 S ATOM 2255 OH2 TIP S 131 73.104 −1.689 21.760 1.00 32.76 S ATOM 2256 OH2 TIP S 133 101.510 19.036 −1.083 1.00 28.30 S ATOM 2257 OH2 TIP S 134 65.138 6.209 20.472 1.00 27.43 S ATOM 2258 OH2 TIP S 135 94.509 36.623 −12.734 1.00 40.27 S ATOM 2259 OH2 TIP S 136 76.896 11.412 −17.698 1.00 37.17 S ATOM 2260 OH2 TIP S 137 97.379 7.497 −6.673 1.00 41.53 S ATOM 2261 OH2 TIP S 138 62.239 17.934 24.368 1.00 34.35 S ATOM 2262 OH2 TIP S 139 69.630 14.360 −10.771 1.00 38.17 S ATOM 2263 OH2 TIP S 140 84.554 44.493 −2.658 1.00 24.74 S ATOM 2264 OH2 TIP S 141 94.631 8.129 −9.752 1.00 35.45 S ATOM 2265 OH2 TIP S 142 78.415 1.021 3.883 1.00 28.60 S ATOM 2266 OH2 TIP S 143 99.830 12.987 −10.148 1.00 35.79 S ATOM 2267 OH2 TIP S 144 71.235 20.688 11.365 1.00 51.52 S ATOM 2268 OH2 TIP S 145 87.138 25.623 11.165 1.00 41.92 S ATOM 2269 OH2 TIP S 146 60.803 15.332 23.294 1.00 32.69 S ATOM 2270 OH2 TIP S 148 73.970 32.165 −13.455 1.00 33.99 S ATOM 2271 OH2 TIP S 149 88.146 19.004 17.326 1.00 27.60 S ATOM 2272 OH2 TIP S 150 90.803 9.970 18.127 1.00 35.03 S ATOM 2273 OH2 TIP S 153 86.261 32.393 −16.403 1.00 41.89 S ATOM 2274 OH2 TIP S 155 102.147 7.767 −0.215 1.00 38.83 S ATOM 2275 OH2 TIP S 159 95.238 0.811 −7.614 1.00 47.22 S ATOM 2276 OH2 TIP S 163 92.356 36.543 −5.580 1.00 40.19 S ATOM 2277 OH2 TIP S 172 66.640 4.633 22.314 1.00 29.95 S ATOM 2278 OH2 TIP S 176 99.303 9.124 3.136 1.00 37.07 S ATOM 2279 OH2 TIP S 184 104.566 20.517 −7.318 1.00 40.83 S ATOM 2280 OH2 TIP S 185 90.295 6.390 −15.433 1.00 34.81 S ATOM 2281 OH2 TIP S 186 82.626 12.831 8.023 1.00 23.99 S ATOM 2282 OH2 TIP S 187 86.159 18.737 24.618 1.00 32.12 S ATOM 2283 OH2 TIP S 188 79.867 7.010 −7.877 1.00 28.52 S ATOM 2284 OH2 TIP S 189 88.469 4.967 1.404 1.00 45.39 S ATOM 2285 OH2 TIP S 190 95.628 28.435 −17.705 1.00 31.73 S ATOM 2286 OH2 TIP S 191 76.228 7.822 28.547 1.00 36.76 S ATOM 2287 OH2 TIP S 192 85.930 8.936 23.323 1.00 31.58 S ATOM 2288 OH2 TIP S 193 73.669 24.555 −14.317 1.00 34.12 S ATOM 2289 OH2 TIP S 194 99.847 12.959 4.319 1.00 43.06 S ATOM 2290 OH2 TIP S 195 76.225 28.669 −3.386 1.00 38.83 S ATOM 2291 OH2 TIP S 197 76.955 24.214 20.057 1.00 35.16 S ATOM 2292 OH2 TIP S 198 65.723 11.313 28.926 1.00 38.40 S ATOM 2293 OH2 TIP S 199 88.482 28.463 4.472 1.00 29.21 S ATOM 2294 OH2 TIP S 200 71.017 17.440 −13.980 1.00 37.15 S ATOM 2295 OH2 TIP S 201 64.967 12.265 13.947 1.00 55.03 S ATOM 2296 OH2 TIP S 204 99.611 22.229 −14.818 1.00 46.97 S ATOM 2297 OH2 TIP S 205 65.422 −1.944 20.970 1.00 65.13 S ATOM 2298 OH2 TIP S 210 89.648 5.683 12.672 1.00 38.65 S ATOM 2299 OH2 TIP S 213 80.842 40.555 7.721 1.00 37.38 S ATOM 2300 OH2 TIP S 214 77.452 22.142 23.411 1.00 36.35 S ATOM 2301 OH2 TIP S 216 104.280 21.111 −10.347 1.00 35.15 S ATOM 2302 OH2 TIP S 225 84.900 44.787 −5.575 1.00 36.10 S ATOM 2303 OH2 TIP S 230 74.759 19.808 9.165 1.00 29.67 S ATOM 2304 OH2 TIP S 231 76.375 2.991 −2.919 1.00 33.34 S ATOM 2305 OH2 TIP S 232 97.252 36.990 −15.430 1.00 39.17 S ATOM 2306 OH2 TIP S 233 70.180 4.692 8.907 1.00 29.97 S ATOM 2307 OH2 TIP S 234 96.055 11.349 −8.926 1.00 29.40 S ATOM 2308 OH2 TIP S 235 70.916 31.535 4.186 1.00 53.99 S ATOM 2309 OH2 TIP S 236 83.279 23.905 15.245 1.00 40.79 S ATOM 2310 OH2 TIP S 237 90.441 34.500 3.752 1.00 37.91 S ATOM 2311 OH2 TIP S 238 74.369 15.521 −11.954 1.00 36.85 S ATOM 2312 OH2 TIP S 239 82.630 5.971 5.382 1.00 48.63 S ATOM 2313 OH2 TIP S 240 101.866 29.649 1.029 1.00 48.93 S ATOM 2314 O12 GLC G 2 74.980 15.310 28.834 1.00 58.25 G ATOM 2315 C11 GLC G 2 74.113 15.072 27.724 1.00 58.49 G ATOM 2316 C13 GLC G 2 74.885 14.362 26.609 1.00 58.11 G ATOM 2317 O14 GLC G 2 73.990 14.120 25.524 1.00 58.57 G ATOM 2318 C15 GLC G 2 75.438 13.023 27.096 1.00 57.55 G ATOM 2319 O16 GLC G 2 74.357 12.183 27.507 1.00 57.24 G ATOM 2320 O12 GLC G 3 68.191 4.312 13.268 1.00 63.76 G ATOM 2321 C11 GLC G 3 67.998 3.273 14.231 1.00 63.57 G ATOM 2322 C13 GLC G 3 69.274 2.429 14.330 1.00 64.06 G ATOM 2323 O14 GLC G 3 69.570 1.858 13.049 1.00 62.75 G ATOM 2324 C15 GLC G 3 69.094 1.303 15.364 1.00 63.85 G ATOM 2325 O16 GLC G 3 68.010 0.444 14.978 1.00 65.65 G ATOM 2326 O12 GLC G 4 87.921 37.473 −13.378 1.00 46.73 G ATOM 2327 C11 GLC G 4 88.767 36.757 −14.265 1.00 46.84 G ATOM 2328 C13 GLC G 4 90.050 36.439 −13.526 1.00 46.74 G ATOM 2329 O14 GLC G 4 90.660 37.648 −13.104 1.00 46.91 G ATOM 2330 C15 GLC G 4 90.999 35.678 −14.435 1.00 47.60 G ATOM 2331 O16 GLC G 4 92.193 35.413 −13.700 1.00 50.48 G ATOM 2332 O12 GLC G 6 78.608 8.519 28.683 1.00 42.02 G ATOM 2333 C11 GLC G 6 79.227 8.721 29.956 1.00 44.70 G ATOM 2334 C13 GLC G 6 80.218 9.877 29.849 1.00 45.13 G ATOM 2335 O14 GLC G 6 81.208 9.537 28.896 1.00 47.43 G ATOM 2336 C15 GLC G 6 80.904 10.129 31.180 1.00 46.92 G ATOM 2337 O16 GLC G 6 81.611 8.950 31.564 1.00 49.38 G ATOM 2338 O12 GLC G 8 83.278 5.163 12.485 1.00 46.74 G ATOM 2339 C11 GLC G 8 82.460 3.987 12.559 1.00 50.09 G ATOM 2340 C13 GLC G 8 83.236 2.894 13.286 1.00 50.09 G ATOM 2341 O14 GLC G 8 84.408 2.621 12.529 1.00 50.75 G ATOM 2342 C15 GLC G 8 82.412 1.597 13.414 1.00 52.04 G ATOM 2343 O16 GLC G 8 82.051 1.062 12.130 1.00 53.37 G ATOM 2344 O12 GLC G 10 87.146 4.682 −5.006 1.00 25.46 G ATOM 2345 C11 GLC G 10 85.823 5.086 −5.356 1.00 27.64 G ATOM 2346 C13 GLC G 10 85.782 5.498 −6.835 1.00 30.79 G ATOM 2347 O14 GLC G 10 86.689 6.600 −7.069 1.00 29.47 G ATOM 2348 C15 GLC G 10 84.354 5.916 −7.219 1.00 30.60 G ATOM 2349 O16 GLC G 10 83.947 7.022 −6.417 1.00 31.23 G ATOM 2350 CBI DRG L 1 82.223 19.878 9.473 1.00 17.56 L ATOM 2351 OBH DRG L 1 82.835 19.573 10.730 1.00 20.33 L ATOM 2352 CBG DRG L 1 82.419 20.512 11.733 1.00 17.87 L ATOM 2353 CBF DRG L 1 83.661 21.291 12.177 1.00 16.47 L ATOM 2354 NBK DRG L 1 84.171 22.133 11.085 1.00 15.68 L ATOM 2355 CBJ DRG L 1 83.683 23.479 10.751 1.00 12.47 L ATOM 2356 CBE DRG L 1 84.739 20.294 12.600 1.00 16.76 L ATOM 2357 CBA DRG L 1 84.178 19.405 13.715 1.00 18.27 L ATOM 2358 OBB DRG L 1 82.790 19.632 14.017 1.00 18.03 L ATOM 2359 CBC DRG L 1 81.853 19.747 12.937 1.00 18.62 L ATOM 2360 CBD DRG L 1 80.732 20.611 13.524 1.00 14.59 L ATOM 2361 NAW DRG L 1 81.398 18.547 12.551 1.00 18.60 L ATOM 2362 CAX DRG L 1 80.185 18.344 12.014 1.00 15.55 L ATOM 2363 CAY DRG L 1 79.107 19.141 11.643 1.00 13.82 L ATOM 2364 CAZ DRG L 1 77.988 18.555 11.053 1.00 16.37 L ATOM 2365 CAP DRG L 1 77.930 17.180 10.830 1.00 15.88 L ATOM 2366 CAO DRG L 1 78.999 16.366 11.196 1.00 15.07 L ATOM 2367 CAN DRG L 1 80.107 16.973 11.783 1.00 17.80 L ATOM 2368 CAM DRG L 1 81.290 16.377 12.187 1.00 19.34 L ATOM 2369 CAH DRG L 1 81.811 15.087 12.083 1.00 19.93 L ATOM 2370 CAV DRG L 1 82.083 17.407 12.657 1.00 18.53 L ATOM 2371 CAU DRG L 1 83.404 17.144 13.014 1.00 18.70 L ATOM 2372 NAT DRG L 1 84.365 17.964 13.438 1.00 17.82 L ATOM 2373 CAS DRG L 1 85.523 17.317 13.610 1.00 15.80 L ATOM 2374 CAR DRG L 1 86.807 17.682 14.000 1.00 14.23 L ATOM 2375 CAQ DRG L 1 87.803 16.708 14.047 1.00 13.92 L ATOM 2376 CAI DRG L 1 87.526 15.384 13.714 1.00 16.21 L ATOM 2377 CAJ DRG L 1 86.244 15.003 13.324 1.00 16.43 L ATOM 2378 CAK DRG L 1 85.264 15.988 13.278 1.00 17.76 L ATOM 2379 CAL DRG L 1 83.932 15.867 12.904 1.00 18.99 L ATOM 2380 CAG DRG L 1 83.130 14.829 12.439 1.00 19.47 L ATOM 2381 CAC DRG L 1 83.403 13.472 12.290 1.00 18.70 L ATOM 2382 OAB DRG L 1 84.471 12.895 12.480 1.00 18.10 L ATOM 2383 NAD DRG L 1 82.277 12.904 11.856 1.00 18.49 L ATOM 2384 CAE DRG L 1 81.128 13.799 11.622 1.00 20.08 L ATOM 2385 OAF DRG L 1 80.902 13.891 10.214 1.00 24.92 L ATOM 2386 S SO4 I 1 64.638 8.174 16.414 1.00 89.13 I ATOM 2387 O1 SO4 I 1 65.311 9.465 16.666 1.00 88.78 I ATOM 2388 O2 SO4 I 1 63.197 8.413 16.200 1.00 89.62 I ATOM 2389 O3 SO4 I 1 64.827 7.262 17.566 1.00 88.49 I ATOM 2390 O4 SO4 I 1 65.197 7.555 15.196 1.00 89.77 I ATOM 2391 S SO4 I 3 84.884 −1.751 12.531 1.00 81.17 I ATOM 2392 O1 SO4 I 3 84.762 −0.302 12.775 1.00 81.32 I ATOM 2393 O2 SO4 I 3 84.538 −2.490 13.758 1.00 81.49 I ATOM 2394 O3 SO4 I 3 86.280 −2.053 12.162 1.00 81.73 I ATOM 2395 O4 SO4 I 3 83.976 −2.163 11.440 1.00 81.19 I ATOM 2396 S SO4 I 5 74.420 22.898 12.677 1.00 85.50 I ATOM 2397 O1 SO4 I 5 73.256 22.153 12.161 1.00 85.36 I ATOM 2398 O2 SO4 I 5 75.637 22.104 12.412 1.00 84.51 I ATOM 2399 O3 SO4 I 5 74.250 23.138 14.126 1.00 84.13 I ATOM 2400 O4 SO4 I 5 74.527 24.202 11.997 1.00 85.44 I ATOM 2401 S SO4 I 6 68.798 6.993 −3.457 1.00 73.84 I ATOM 2402 O1 SO4 I 6 68.338 7.338 −4.823 1.00 72.86 I ATOM 2403 O2 SO4 I 6 69.298 8.206 −2.791 1.00 73.61 I ATOM 2404 O3 SO4 I 6 69.888 6.003 −3.540 1.00 73.52 I ATOM 2405 O4 SO4 I 6 67.690 6.426 −2.658 1.00 73.19 I ATOM 2406 O2 PO4 P 100 66.501 25.721 2.616 1.00 85.98 P ATOM 2407 O3 PO4 P 100 64.376 25.028 1.654 1.00 86.96 P ATOM 2408 O4 PO4 P 100 65.755 26.653 0.496 1.00 86.51 P ATOM 2409 O1 PO4 P 100 64.621 27.279 2.570 1.00 86.98 P ATOM 2410 P PO4 P 100 65.315 26.170 1.832 1.00 87.36 P ATOM 2411 S SO4 X 3 80.775 −0.045 7.874 0.50 22.29 X ATOM 2412 O1 SO4 X 3 81.160 0.521 9.176 0.50 22.30 X ATOM 2413 O2 SO4 X 3 81.320 −1.407 7.778 0.50 22.49 X ATOM 2414 O3 SO4 X 3 81.309 0.781 6.777 0.50 23.26 X ATOM 2415 O4 SO4 X 3 79.305 −0.088 7.772 0.50 24.36 X END 

1. A method for selecting a compound for modulating the activity of phosphoinositide dependent protein kinase 1 (PDK1), the method comprising: [i] generating a three-dimensional structure of the protein kinase catalytic domain of PDK1 as defined by Example 2, 3, 7 or 8; [ii] identifying predicted binding region(s): the PDK1 Interacting Fragment (PIF) binding pocket formed by residues including residues Lys115, Ile118, Ile119 on the αB helix, Val124, Val127 on the αC helix, and Leu 155 on β-sheet 5 of full length human PDK1 as set forth in SEQ ID NO: 3, the “phosphate binding pocket” formed by residues including residues Lys76, Arg131, Thr148 and Gln150 of full length human PDK1 as set forth in SEQ ID NO: 3, and/or the αC helix formed by residues 123-136 of full length human PDK1 as set forth in SEQ ID NO: 3 in any of the models generated in step [i]; [iii] modeling a plurality of three-dimensional structures of candidate compounds; [iv] comparing said three-dimensional structure of the protein kinase catalytic domain of PDK1 binding regions/pockets as identified in step [ii] with the three-dimensional structure of each of said candidate compounds of step [iii]; and [v] selecting one of the candidate compounds as a compound for modulating the activity of phosphoinositide dependent protein kinase 1 (PDK1).
 2. The method of claim 1 wherein the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 structure is a three-dimensional structure (or part thereof) determined for a polypeptide consisting of residues 51 to 359 of full length human PDK1 as set forth in SEQ ID NO:
 3. 3. The method of claim 2 wherein the three-dimensional structure (or part thereof) is determined for a polypeptide consisting of residues 51 to 359 of full length human PDK1 as set forth in SEQ ID NO: 3 and the amino acid sequence Gly-Pro preceding the methionine corresponding to Met51 of human PDK1.
 4. The method of claim 1 wherein the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 structure is a three-dimensional structure (or part thereof) determined for a polypeptide consisting of residues 71 to 359 of full length human PDK1 as set forth in SEQ ID NO: 3 or a fusion thereof.
 5. The method of claim 1 wherein the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 structure is obtainable by X-ray analysis of a crystal obtainable using a mother liquor solution comprising ammonium sulphate.
 6. The method of claim 5 wherein the mother liquor solution is of pH 7 to
 9. 7. The method of claim 6 wherein the mother liquor solution is of pH 8.5.
 8. The method of claim 7 wherein the mother liquor solution comprises ATP.
 9. The method of claim 1 wherein the compound is for modulating the protein kinase activity of PDK1 towards protein kinase B (PKB) or other pleckstrin homology (PH)-domain-comprising/phosphoinositide-binding substrate of PDK1.
 10. The method of claim 1 wherein the compound is for modulating the protein kinase activity of PDK1 towards serum and glucocorticoid stimulated protein kinase (SGK), S6 kinase (S6K) or other substrate of PDK1 whose phosphorylation by PDK1 is promoted by phosphorylation of the substrate on the Ser/Thr of the “hydrophobic motif” FXXFS/TY as set forth in SEQ ID NO:
 2. 11. The method of claim 1 further comprising the step of synthesising, purifying and/or formulating the compound.
 12. The method of claim 1, wherein the method further comprises: designing one or more of said molecules prior to modelling.
 13. A method for selecting a compound for modulating the activity of PDK1 Interacting Fragment (PIF) binding pocket containing protein kinase, the method comprising: [i] modeling a three-dimensional structure of a plurality of molecules in a computer; [ii] generating a three-dimensional structure of the protein kinase catalytic domain of PDK1 as defined by Example 2, 3, 7 or 8; [iii] comparing the three-dimensional structure of each of said molecules with the three-dimensional structure of said phosphate binding pocket of human PDK1 and optionally also said hydrophobic pocket of human PDK1; [iv] identifying a molecule from the plurality of the modeled molecules which binds to said PIF binding pocket in the position equivalent to a hydrophobic pocket of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and Leu155 of full-length human PDK1 as set forth in SEQ ID NO: 3, and/or a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and Gln150 of SEQ ID NO: 3; and [v] selecting one of the modeled molecules as said compound based on a predicted ability of the molecule to interact with said phosphate binding pocket of protein kinase or said hydrophobic pocket of protein kinase, wherein the three-dimensional structure or a part thereof is determined for a polypeptide comprising residues 51 to 359 of full length human PDK1 as set forth in SEQ ID NO:
 3. 14. The method of claim 13, wherein the method further comprises: designing one or more of said molecules prior to modelling. 